Phl post
Author: a | 2025-04-23
Auto-Track PHL Post Shipments. Our Multi-Carrier Tracking API will auto-track your PHL Post shipments. PHL Post Post-Shipping Automation. Fully integrate PHL Post tracking into your
PHL Post – Philipphine Post - Post Parcel
[M] /home/pi/linktp/rtl8852au/core/crypto/sha256.o CC [M] /home/pi/linktp/rtl8852au/core/crypto/sha256-prf.o CC [M] /home/pi/linktp/rtl8852au/core/crypto/rtw_crypto_wrap.o CC [M] /home/pi/linktp/rtl8852au/core/rtw_swcrypto.o CC [M] /home/pi/linktp/rtl8852au/core/rtw_trx_usb.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_init.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_debug.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_tx.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_rx.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_rx_agg.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_api_drv.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_role.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_sta.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_mr.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_sec.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_chan.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_sw_cap.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_util.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_pkt_ofld.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_connect.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_chan_info.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_wow.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_dm.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_chnlplan.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_country.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_chnlplan_6g.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_regulation.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_regulation_6g.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_led.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_trx_mit.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_acs.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_mcc.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_ecsa.o CC [M] /home/pi/linktp/rtl8852au/phl/test/phl_dbg_cmd.o CC [M] /home/pi/linktp/rtl8852au/phl/test/phl_ps_dbg_cmd.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_msg_hub.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_sound.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_twt.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_notify.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_sound_cmd.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_p2pps.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_ps.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_thermal.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_cmd_dispatch_engine.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_cmd_dispatcher.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_cmd_dispr_controller.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_cmd_ser.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_cmd_general.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_cmd_scan.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_cmd_btc.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_cmd_ps.o CC [M] /home/pi/linktp/rtl8852au/phl/phl_watchdog.o CC [M] /home/pi/linktp/rtl8852au/phl/hci/phl_trx_usb.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_api_mac.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_api_bb.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_api_rf.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_api_btc.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_api_efuse.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_com_i.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_init.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_io.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_rx.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_tx.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_sta.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_cam.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_csi_buffer.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_beamform.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_sound.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_chan.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_str_proc.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_fw.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_cap.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_ser.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_ps.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_c2h.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_dbcc.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_chan_info.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_wow.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_ld_file.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_regulation.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_led.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_trx_mit.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_acs.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_mcc.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_api.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_twt.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_notify.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_p2pps.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_thermal.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/hal_usb.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/efuse/hal_efuse.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/addr_cam.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/cmac_tx.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/coex.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/cpuio.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/dbgpkg.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/dbgport_hw.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/dbg_cmd.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/dle.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/efuse.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/fwcmd.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/fwdl.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/fwofld.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/gpio.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/hci_fc.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/hdr_conv.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/hw_seq.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/h2c_agg.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/hw.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/hwamsdu.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/init.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/la_mode.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/mcc.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/mport.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/phy_rpt.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/power_saving.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/pwr.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/p2p.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/role.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/rx_filter.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/rx_forwarding.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/ser.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/security_cam.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/sounding.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/status.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/tblupd.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/tcpip_checksum_offload.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/trx_desc.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/trxcfg.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/twt.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/wowlan.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/flash.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/spatial_reuse.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/pwr_seq_func.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/phy_misc.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/_usb.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/mac_8852a/gpio_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/mac_8852a/init_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/mac_8852a/pwr_seq_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/mac_ax/mac_8852a/_usb_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/fw_ax/rtl8852a/hal8852a_fw.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/mac/fw_ax/rtl8852a/hal8852a_fw_log.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/btc/hal_btc.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/btc/halbtc_def.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/btc/halbtc_action.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/btc/halbtc_fw.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/btc/halbtc_dbg_cmd.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/btc/btc_8852a/btc_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/rtl8852a/rtl8852a_halinit.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/rtl8852a/rtl8852a_mac.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/rtl8852a/rtl8852a_cmd.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/rtl8852a/rtl8852a_phy.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/rtl8852a/rtl8852a_ops.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/rtl8852a/hal_trx_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/rtl8852a/usb/rtl8852au_halinit.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/rtl8852a/usb/rtl8852au_halmac.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/rtl8852a/usb/rtl8852au_io.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/rtl8852a/usb/rtl8852au_led.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/rtl8852a/usb/rtl8852au_ops.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/rtl8852a/usb/hal_trx_8852au.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_api.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_rua_tbl.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_auto_dbg.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_cfo_trk.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_ch_info.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_cmn_rpt.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_dbcc.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_dbg.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_dbg_cmd.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_dfs.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_edcca.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_env_mntr.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_hw_cfg.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_init.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_interface.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_la_mode.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_math_lib.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_mp.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_plcp_gen.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_plcp_tx.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_pmac_setting.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_psd.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_physts.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_pwr_ctrl.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_ra.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_statistics.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_ant_div.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_dig.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_fwofld.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_dyn_csi_rsp.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a/halbb_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a/halbb_8852a_api.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a/halbb_hwimg_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a/halbb_reg_cfg_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a_2/halbb_8852a_2.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a_2/halbb_8852a_2_api.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a_2/halbb_hwimg_8852a_2.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a_2/halbb_reg_cfg_8852a_2.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_pmac.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_api.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_dbg.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_dbg_cmd.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_ex.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_hw_cfg.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_init.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_interface.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_pwr_table.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_iqk.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_8852a_api.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_hwimg_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_txgapk_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_iqk_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_reg_cfg_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_dpk_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_dack_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_set_pwr_table_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_efuse_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_tssi_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_kfree_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_psd_8852a.o LD [M] /home/pi/linktp/rtl8852au/8852au.o MODPOST /home/pi/linktp/rtl8852au/Module.symvers CC [M] /home/pi/linktp/rtl8852au/8852au.mod.o LD [M] /home/pi/linktp/rtl8852au/8852au.ko make[1]: Leaving directory '/usr/src/linux-headers-5.10.103+' #cp Module.symvers .symvers.8852au ➜ rtl8852au git:(dwa-x1850) ✗ make install install -p -m 644 8852au.ko /lib/modules/5.10.103+/kernel/drivers/net/wireless/realtek/rtw89/ /sbin/depmod -a 5.10.103+ ➜ rtl8852au git:(dwa-x1850) ✗ reboot ➜ rtl8852au git:(dwa-x1850) ✗ airmon-ng PHY Interface Driver Chipset ```Philippines Post Office (PHL Post) Holidays 2025
80 Å (Hu and Liu 2015).Ligands have higher transition energy than protein which is read as a higher molar absorption coefficient (ε) value of PHL, each PHL and INS have the ε value 7092 and 1389·M-1·cm-1 (Table 1). An interaction between INS and PHL can be proposed based on spectrum and the ε value. The largest ε value was obtained at the mole ratio of 1:0.05 (PHL: INS), which was 159,040·M-1·cm-1. The lowest ε value was found in the ratio 1:1 is 9396·M-1·cm-1. The higher the mole ratio of INS, the higher the absorbance, but the weaker the ability to capture light or the smaller the molar absorption coefficient. In this study, the maximum absorbance of PHL was 285 nm (Fig. 1a). Similarly, the optimum PHL absorption was detected at a wavelength of 285 nm (Chen et al. 2020). The optimum absorption peak followed the PHL trend than INS, an indication that the increase in absorbance of the INS–PHL mixture is dominantly influenced by PHL even though the PHL mole ratio is constant. Albumin binding with ligands was conditioned with low ligand concentration but a high ligand–albumin ratio. Ligand molecules can associate with low affinity (Tang et al. 2006). Figure 1b showed that INS–PHL absorption increased with increasing PHL concentration. The higher the PHL ratio, the larger the wavelength shift of the shape of peak and maximum absorbency of INS.Table 1 The molar absorption coefficients (ε) of PHL and INSFull size tableProtein absorbance measurements have been carried out at room temperature conditions and normal pH to mimic protein’s normal condition (Nienhaus and Nienhaus 2005). In two separate studies, it was found that insulin does not dissolve at normal pH but dissolves in the pH range 2–3 using HCl as a solvent (Gooch 2004; Sigma-Aldrich Co. 2014). The intrinsic fluorescence in insulin fibrils was recorded at pH 1.8 and pH 7, which was different from normal protein. This study used HCl pH 2 as a solvent. The morphological review of insulin using TEM showed that insulin fluorescence was not entirely related to the morphological features of amyloid fibrils (Iannuzzi et al.. Auto-Track PHL Post Shipments. Our Multi-Carrier Tracking API will auto-track your PHL Post shipments. PHL Post Post-Shipping Automation. Fully integrate PHL Post tracking into yourPHL : ethics - Post University - Course Hero
Fluorescence properties of INS mainly come from Tyr residues (A14, A19, B16, B26). Therefore, the fluorescence properties of Tyr were also studied in the absence and presence of PHL (Fig. 7). The spectrum was recorded at an excitation wavelength ranging from 280 to 400 nm and a temperature of 298 K, while the Tyr residues were measured at 305 nm. Figure 7 shows that the addition of different PHL concentrations can change the fluorescence intensity of Tyr significantly. As the concentration of PHL increases, the fluorescence intensity of Tyr weakens and produces a redshift. This result is similar to the fluorescence quenching experiment of INS by PHL. It confirms that PHL can change Tyr residues’ surrounding environment and decrease fluorescence intensity.Fig. 7The fluorescence intensity of Tyr by PHL in 298KFull size imageDetermination of binding constant of INS–PHL interactionINS’s quenching effect by PHL has been known as static quenching and accompanied by dynamic quenching, indicating interactions and the formation of complexes between INS and PHL. Static quenching takes into account the formation of INS–PHL interaction. The researchers (Lakowicz 1999; Zhang et al. 2008; Gentili et al. 2008; Shi et al. 2013; Shi et al. 2015; Hashemi-Shahraki et al. 2020) explained that the binding constant (Ka) value and the number of binding sites (n) between biomacromolecules and small molecules can be determined by Eq. 1.$$ \log \left[\frac{F_0-F}{F}\right]=\log {K}_a+n\log \left[Q\right] $$ (2) F0: Fluorescence intensity without adding quencherF: Fluorescence intensity with a particular concentration of quenching agentKa: Binding constant of two molecules (M-1)n: Binding site of two molecules[Q]:The concentration of quenching agent (μM)The Ka values of the INS–PHL interaction were found to be 1.53 × 104, 1.16 × 104, and 9.80 × 103 M−1 at 288, 298, and 308 K, respectively (Eq. 2). The calculated Ka values indicate that INS and PHL are mutually binding, and the binding effect is relatively significant. Based on Table 2, the Ka values decreased with the increase of temperature. It means that INS and PHL’s stability reduces at a higher temperature, similar to the observation by Lakowicz and Weber (1973). An increase in the temperature can decrease The spectrum (Soleymani et al. 2016). In the present study, PHL was used as a quenching agent and interacted at different ratios. Measurements were set with a wavelength of 280 nm at three temperatures, namely 288 K, 298 K, and 308 K (Figs. 3, 4, 5). Figures 3, 4, and 5 show that the maximum INS emission signal was observed at a wavelength of 305 nm, indicating that temperature changes did not affect the INS emission signal.Fig. 3The fluorescence intensity of INS and PHL in 288 KFull size imageFig. 4The fluorescence intensity of INS and PHL in 298 KFull size imageFig. 5The fluorescence intensity of INS and PHL in 308 KFull size imageInternal fluorescence effects (IFE) has been corrected by equations (Farajzadeh-Dehkordi et al. 2020; Hashemi-Shahraki et al. 2020; Wani et al. 2020b).$$ {F}_{\mathrm{corr}}={F}_{\mathrm{obs}}\times {e}^{\frac{A_{\mathrm{ex}}+{A}_{\mathrm{em}}}{2}} $$ (1) Fcorr and Fobs are the correction and observation of fluorescence intensities, respectively. Aex and Aem are the wavelengths of excitation and emission, respectively. The Aex and Aem were 280 nm and 305 nm. The fluorescence intensity ratio (\( \raisebox{1ex}{${F}_0$}\!\left/ \!\raisebox{-1ex}{$F$}\right. \)) at different temperatures was also calculated. F0 and F are ascribed as the fluorescence intensity of INS before and after the addition of quencher (PHL), respectively. The highest ratio of 8.24 was obtained at 288 K, followed by 7.78 at 298 K. When the temperature increased to 308 K, it resulted in the lowest ratio of 7.52. These results suggest that the fluorescence intensity ratio \( \raisebox{1ex}{${F}_0$}\!\left/ \!\raisebox{-1ex}{$F$}\right. \) decreases with the increased temperature.Figure 6 shows the plotting curve of the concentration of PHL against the fluorescence intensity. It can be observed that the quenching effect occurs at the three temperatures. The addition of PHL causes changes in the microenvironment surrounding the INS’s amino acid residues, resulting in a decrease in INS’s fluorescence intensity, which indicates an interaction between INS and PHL. The mechanism of action from these interactions can be further judged through the Stern-Volmer equation.Fig. 6The fluorescence intensity plotted of PHL at different temperaturesFull size imageThe influence of PHL on the fluorescence intensity of TyrIt has been proposed that theDumaguete PHL Post Postal ID Processing and Requirements
Using AutoDock MGL Tools, AutoDock Vina, Pymol visualization tool, and LigPlot+ version V.2.2.4. Simulations were performed on human insulin 3i40 obtained from the protein databank and phloretin molecules were drawn using ACD ChemSketch 2019.1.2.ConclusionsUV/Vis spectra showed that the interaction between PHL and INS produced strong absorption at a wavelength of 282 nm. The chromophore group of the aromatic amino acid ring has an absorption overlap with the PHL chromophore group. PHL and INS interactions occur at lower wavelengths with higher energies (blue shift and hyperchromic). The fluorescence analysis results showed that the excitation and emission occurred at a wavelength of 280 nm and 305 nm. Temperature changes did not affect INS emissions. However, the interactions of PHL and INS caused a 305–317-nm redshift. Temperature affected the binding constant (Ka) and the binding site (n). Ka decreased with increasing temperature and vice versa, but the binding site value increased. An indication that the stability of PHL and INS interactions is temperature dependent. The thermodynamic parameters such as enthalpy (ΔH0) and entropy (ΔS0) each have a value of − 16,514 kJ/mol and 22.65 J/mol·K. PHL and INS interaction formed hydrogen bonds and were hydrophobic. The free energy (ΔG0) values at all temperatures (288 K, 298 K, and 308 K) were − 23.04, − 23.26, and − 23.49 kJ/mol, respectively. PHL and INS interactions took place spontaneously. The quenching effect was dynamic and static. KD values (1.18 × 106, 1.13 × 106, and 1.12 × 106 M-1) were greater than those of KS (1.64 × 104, 1.62 × 104, and 1.60 × 104 M-1). The higher the temperature, the less KD and KS. The appearance of two negative signals on circular dichroism (CD) spectropolarimeter indicates the α-helix structure. The addition of PHL has revealed the proportion of α-helix in the insulin structure. PHL could stabilize the structure of insulin, indicating that phloretin induced regional configuration changes in insulin. Phloretin and insulin interacted and formed a complex. Furthermore, the stabilization of phloretin and enhancement of the α-helix structural configuration in insulin could be related to the phenomenon that phloretin can improve insulin resistance. AvailabilityPHL 203.32 : Ethics - Post University - Course Hero
Insulin by the circular dichroism spectroscopy and explore whether the addition of phloretin can stabilize the secondary structure of insulin. The study’s outcome has potential application in medical research and the treatment of diabetic patients.Materials and methodsThe materials used in this study included insulin (99%) CAS 30003-72-6, L-tyrosine (98%) CAS 60-18-4, and phloretin (99%) CAS 60-82-2 (purchased from Sigma Aldrich), hydrochloric acid (pH = 2.0) CAS 7722-84-1, methanol 99.5% (Merck), and distilled water. The instruments utilized were ultrasonic vibration machine, UV/visible spectrometer (PerkinElmer Lambda 265), fluorescence spectrometer (Jasco FP-750 with Xenon as a fluorescent light source), constant temperature water tank (FIRSTEK Model-B403H), fluorescent holder (Jasco STR-312), circular dichroism (CD) spectropolarimeter (Jasco J-815 with a 150-W Xenon lamp as a light source), and a 1-mL quartz cuvette for sample measurement.Spectroscopy UV/Vis analysisSamples of PHL and INS were diluted using HCl (pH = 2.0) and methanol as a solvent. Stock solutions of INS, PHL, and Tyr were made with the following concentrations: 2.9 mg INS with 5 mL HCl, 1.37 mg PHL with 5 mL MeOH, and 0.18 mg Tyr 10 mL HCl. The PHL concentration was maintained constantly at 5.0 × 10−5M, while the INS concentration was gradually increased from 2.5 × 10−6 to 5.0 × 10−5 M. The INS and PHL mixed solutions were made by mixing solutions in various mole ratios of 1:0.05, 1:0.1, 1:0.5, and 1:1 (PHL: INS). The mixture was put into an ultrasonic vibrator for 30 min and transferred to a 1-mL quartz cuvette to record UV/Vis spectrometer measurements. Homogenization was carried out so that the solutions get mixed. In this study, ultrasonic vibrations were used because their energy is lower than the peptide bonds’ breaking energy, composed of strong covalent bonds (Gong et al. 2019). The binding free energy of insulin was − 8.97 ± 1.41 kcal/mol or 9.60692 × 1016 kHz. The frequency of ultrasonic vibrations was 18 − 40 kHz.Fluorescence spectroscopy analysisThe INS and PHL mixed solutions were prepared with different molar ratios of INS: PHL (1:0; 1:0.25; 1:0.5; 1:0.75; 1:1; 1:1.25; 1:1.5; 1:1.75; 1:2; 1:2.25) and put in the ultrasonic vibrator for. Auto-Track PHL Post Shipments. Our Multi-Carrier Tracking API will auto-track your PHL Post shipments. PHL Post Post-Shipping Automation. Fully integrate PHL Post tracking into your 5M views. Discover videos related to Phl Airport Map on TikTok. See more videos about Phl Airport, Phl Post Tracking, Phl Post Package, Phl Channel, Airport Moments, Karl at Airport.Impact of Post-Harvest Loss (PHL) on Food Security:
Aptamer (Verdian-Doghaei and Housaindokht 2015). While wavelength at 260–400 nm is used by Correia et al. (2012). INS has two peaks at 275 nm and 282 nm (Fig. 1a,b). The presence of the two peaks in INS is probably due to the absorption of an amine group having a lone electron pair (275 nm) and an aromatic ring group (282 nm). Lone pair electrons own by NH bonds was a componen of protamine. Protamine is composed of arginine, which is rich in NH bonds. Protamine is a protein that can protect insulin from being degraded by enzymes. The uptake of proteins such as protamine was detected at a wavelength of 275 nm (Nienhaus and Nienhaus 2005). The aromatic ring is owned by tyrosine, tryptophan, and phenylalanine also have a signals. It was seen at a wavelength of 280 nm (Hashemi-Shahraki et al. 2020; Kierdaszuk et al. 1995). Amino acid aromatic chromophore has an absorption range of 230–300 nm (Nienhaus and Nienhaus 2005).Fig. 1Absorption Spectrum of PHL after variation of INS (a), INS after variation of PHL (b)Full size imageWhen binding occurs, the electrons in the INS residue release energy (fluorescence). At the same time, the electrons in the ligand absorb energy, and the spectra overlap. PHL is a flavonoid compound composed of benzene rings. Prosthetic groups with phi electrons such as chlorophyll, carotenoid, flavin, heme, and retinal are sensitive to the polypeptide environment and can even change the protein structure. The benzene group absorption of PHL overlaps with the aromatic ring absorption of INS. The INS–PHL mixture has an overlapping peak at a wavelength of 283 nm, indicating that INS has shifted the PHL peak from 285 to 283 nm (hyperchromic effect). The INS and PHL’s interaction absorbs a large amount of energy at a lower wavelength than PHL. It has been reported that molecular overlap can occur against small molecules with nitrogenous base groups in the DNA chain (Farajzadeh-Dehkordi et al. 2020). The fluorescence emission spectra overlap with the absorbance spectra of the acceptor molecule. Possibility of energy transfer when the donor–acceptor distance is less than 8 nm orComments
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2025-04-12CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_cmn_rpt.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_dbcc.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_dbg.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_dbg_cmd.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_dfs.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_edcca.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_env_mntr.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_hw_cfg.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_init.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_interface.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_la_mode.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_math_lib.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_mp.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_plcp_gen.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_plcp_tx.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_pmac_setting.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_psd.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_physts.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_pwr_ctrl.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_ra.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_statistics.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_ant_div.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_dig.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_fwofld.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_dyn_csi_rsp.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a/halbb_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a/halbb_8852a_api.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a/halbb_hwimg_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a/halbb_reg_cfg_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a_2/halbb_8852a_2.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a_2/halbb_8852a_2_api.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a_2/halbb_hwimg_8852a_2.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/bb/halbb_8852a_2/halbb_reg_cfg_8852a_2.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_pmac.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_api.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_dbg.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_dbg_cmd.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_ex.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_hw_cfg.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_init.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_interface.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_pwr_table.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_iqk.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_8852a_api.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_hwimg_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_txgapk_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_iqk_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_reg_cfg_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_dpk_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_dack_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_set_pwr_table_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_efuse_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_tssi_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_kfree_8852a.o CC [M] /home/pi/linktp/rtl8852au/phl/hal_g6/phy/rf/halrf_8852a/halrf_psd_8852a.o LD [M] /home/pi/linktp/rtl8852au/8852au.o MODPOST /home/pi/linktp/rtl8852au/Module.symvers CC [M] /home/pi/linktp/rtl8852au/8852au.mod.o LD [M] /home/pi/linktp/rtl8852au/8852au.ko make[1]: Leaving directory '/usr/src/linux-headers-5.10.103+' #cp Module.symvers .symvers.8852au ➜ rtl8852au git:(dwa-x1850) ✗ make install install -p -m 644 8852au.ko /lib/modules/5.10.103+/kernel/drivers/net/wireless/realtek/rtw89/ /sbin/depmod -a 5.10.103+ ➜ rtl8852au git:(dwa-x1850) ✗ reboot ➜ rtl8852au git:(dwa-x1850) ✗ airmon-ng PHY Interface Driver Chipset ```
2025-04-2380 Å (Hu and Liu 2015).Ligands have higher transition energy than protein which is read as a higher molar absorption coefficient (ε) value of PHL, each PHL and INS have the ε value 7092 and 1389·M-1·cm-1 (Table 1). An interaction between INS and PHL can be proposed based on spectrum and the ε value. The largest ε value was obtained at the mole ratio of 1:0.05 (PHL: INS), which was 159,040·M-1·cm-1. The lowest ε value was found in the ratio 1:1 is 9396·M-1·cm-1. The higher the mole ratio of INS, the higher the absorbance, but the weaker the ability to capture light or the smaller the molar absorption coefficient. In this study, the maximum absorbance of PHL was 285 nm (Fig. 1a). Similarly, the optimum PHL absorption was detected at a wavelength of 285 nm (Chen et al. 2020). The optimum absorption peak followed the PHL trend than INS, an indication that the increase in absorbance of the INS–PHL mixture is dominantly influenced by PHL even though the PHL mole ratio is constant. Albumin binding with ligands was conditioned with low ligand concentration but a high ligand–albumin ratio. Ligand molecules can associate with low affinity (Tang et al. 2006). Figure 1b showed that INS–PHL absorption increased with increasing PHL concentration. The higher the PHL ratio, the larger the wavelength shift of the shape of peak and maximum absorbency of INS.Table 1 The molar absorption coefficients (ε) of PHL and INSFull size tableProtein absorbance measurements have been carried out at room temperature conditions and normal pH to mimic protein’s normal condition (Nienhaus and Nienhaus 2005). In two separate studies, it was found that insulin does not dissolve at normal pH but dissolves in the pH range 2–3 using HCl as a solvent (Gooch 2004; Sigma-Aldrich Co. 2014). The intrinsic fluorescence in insulin fibrils was recorded at pH 1.8 and pH 7, which was different from normal protein. This study used HCl pH 2 as a solvent. The morphological review of insulin using TEM showed that insulin fluorescence was not entirely related to the morphological features of amyloid fibrils (Iannuzzi et al.
2025-04-09Fluorescence properties of INS mainly come from Tyr residues (A14, A19, B16, B26). Therefore, the fluorescence properties of Tyr were also studied in the absence and presence of PHL (Fig. 7). The spectrum was recorded at an excitation wavelength ranging from 280 to 400 nm and a temperature of 298 K, while the Tyr residues were measured at 305 nm. Figure 7 shows that the addition of different PHL concentrations can change the fluorescence intensity of Tyr significantly. As the concentration of PHL increases, the fluorescence intensity of Tyr weakens and produces a redshift. This result is similar to the fluorescence quenching experiment of INS by PHL. It confirms that PHL can change Tyr residues’ surrounding environment and decrease fluorescence intensity.Fig. 7The fluorescence intensity of Tyr by PHL in 298KFull size imageDetermination of binding constant of INS–PHL interactionINS’s quenching effect by PHL has been known as static quenching and accompanied by dynamic quenching, indicating interactions and the formation of complexes between INS and PHL. Static quenching takes into account the formation of INS–PHL interaction. The researchers (Lakowicz 1999; Zhang et al. 2008; Gentili et al. 2008; Shi et al. 2013; Shi et al. 2015; Hashemi-Shahraki et al. 2020) explained that the binding constant (Ka) value and the number of binding sites (n) between biomacromolecules and small molecules can be determined by Eq. 1.$$ \log \left[\frac{F_0-F}{F}\right]=\log {K}_a+n\log \left[Q\right] $$ (2) F0: Fluorescence intensity without adding quencherF: Fluorescence intensity with a particular concentration of quenching agentKa: Binding constant of two molecules (M-1)n: Binding site of two molecules[Q]:The concentration of quenching agent (μM)The Ka values of the INS–PHL interaction were found to be 1.53 × 104, 1.16 × 104, and 9.80 × 103 M−1 at 288, 298, and 308 K, respectively (Eq. 2). The calculated Ka values indicate that INS and PHL are mutually binding, and the binding effect is relatively significant. Based on Table 2, the Ka values decreased with the increase of temperature. It means that INS and PHL’s stability reduces at a higher temperature, similar to the observation by Lakowicz and Weber (1973). An increase in the temperature can decrease
2025-04-04The spectrum (Soleymani et al. 2016). In the present study, PHL was used as a quenching agent and interacted at different ratios. Measurements were set with a wavelength of 280 nm at three temperatures, namely 288 K, 298 K, and 308 K (Figs. 3, 4, 5). Figures 3, 4, and 5 show that the maximum INS emission signal was observed at a wavelength of 305 nm, indicating that temperature changes did not affect the INS emission signal.Fig. 3The fluorescence intensity of INS and PHL in 288 KFull size imageFig. 4The fluorescence intensity of INS and PHL in 298 KFull size imageFig. 5The fluorescence intensity of INS and PHL in 308 KFull size imageInternal fluorescence effects (IFE) has been corrected by equations (Farajzadeh-Dehkordi et al. 2020; Hashemi-Shahraki et al. 2020; Wani et al. 2020b).$$ {F}_{\mathrm{corr}}={F}_{\mathrm{obs}}\times {e}^{\frac{A_{\mathrm{ex}}+{A}_{\mathrm{em}}}{2}} $$ (1) Fcorr and Fobs are the correction and observation of fluorescence intensities, respectively. Aex and Aem are the wavelengths of excitation and emission, respectively. The Aex and Aem were 280 nm and 305 nm. The fluorescence intensity ratio (\( \raisebox{1ex}{${F}_0$}\!\left/ \!\raisebox{-1ex}{$F$}\right. \)) at different temperatures was also calculated. F0 and F are ascribed as the fluorescence intensity of INS before and after the addition of quencher (PHL), respectively. The highest ratio of 8.24 was obtained at 288 K, followed by 7.78 at 298 K. When the temperature increased to 308 K, it resulted in the lowest ratio of 7.52. These results suggest that the fluorescence intensity ratio \( \raisebox{1ex}{${F}_0$}\!\left/ \!\raisebox{-1ex}{$F$}\right. \) decreases with the increased temperature.Figure 6 shows the plotting curve of the concentration of PHL against the fluorescence intensity. It can be observed that the quenching effect occurs at the three temperatures. The addition of PHL causes changes in the microenvironment surrounding the INS’s amino acid residues, resulting in a decrease in INS’s fluorescence intensity, which indicates an interaction between INS and PHL. The mechanism of action from these interactions can be further judged through the Stern-Volmer equation.Fig. 6The fluorescence intensity plotted of PHL at different temperaturesFull size imageThe influence of PHL on the fluorescence intensity of TyrIt has been proposed that the
2025-04-13Using AutoDock MGL Tools, AutoDock Vina, Pymol visualization tool, and LigPlot+ version V.2.2.4. Simulations were performed on human insulin 3i40 obtained from the protein databank and phloretin molecules were drawn using ACD ChemSketch 2019.1.2.ConclusionsUV/Vis spectra showed that the interaction between PHL and INS produced strong absorption at a wavelength of 282 nm. The chromophore group of the aromatic amino acid ring has an absorption overlap with the PHL chromophore group. PHL and INS interactions occur at lower wavelengths with higher energies (blue shift and hyperchromic). The fluorescence analysis results showed that the excitation and emission occurred at a wavelength of 280 nm and 305 nm. Temperature changes did not affect INS emissions. However, the interactions of PHL and INS caused a 305–317-nm redshift. Temperature affected the binding constant (Ka) and the binding site (n). Ka decreased with increasing temperature and vice versa, but the binding site value increased. An indication that the stability of PHL and INS interactions is temperature dependent. The thermodynamic parameters such as enthalpy (ΔH0) and entropy (ΔS0) each have a value of − 16,514 kJ/mol and 22.65 J/mol·K. PHL and INS interaction formed hydrogen bonds and were hydrophobic. The free energy (ΔG0) values at all temperatures (288 K, 298 K, and 308 K) were − 23.04, − 23.26, and − 23.49 kJ/mol, respectively. PHL and INS interactions took place spontaneously. The quenching effect was dynamic and static. KD values (1.18 × 106, 1.13 × 106, and 1.12 × 106 M-1) were greater than those of KS (1.64 × 104, 1.62 × 104, and 1.60 × 104 M-1). The higher the temperature, the less KD and KS. The appearance of two negative signals on circular dichroism (CD) spectropolarimeter indicates the α-helix structure. The addition of PHL has revealed the proportion of α-helix in the insulin structure. PHL could stabilize the structure of insulin, indicating that phloretin induced regional configuration changes in insulin. Phloretin and insulin interacted and formed a complex. Furthermore, the stabilization of phloretin and enhancement of the α-helix structural configuration in insulin could be related to the phenomenon that phloretin can improve insulin resistance. Availability
2025-04-10