[Objectives] This study was conducted to optimize the ethanol extraction technology of monoester alkaloids from Radix Aconiti Preparata. [Methods]On the basis of defined extraction times,ethanol concentration,ethanol ...[Objectives] This study was conducted to optimize the ethanol extraction technology of monoester alkaloids from Radix Aconiti Preparata. [Methods]On the basis of defined extraction times,ethanol concentration,ethanol times and extraction time were investigated by HPLC-MS combined with orthogonal test to optimize extraction process using the content of monoester alkaloids( the sum of benzoyl neoaconitine,benzoyl hypoaconitine and benzoyl aconitine) as an index.[Results]The optimum ethanol extraction technology was as follows: 75% ethanol,ethanol amount 25 times of the medicinal material,and each extraction for 1. 5 h.[Conclusions] The optimal extraction technology is simple,feasible,stable and reliable. It can provide reference for the industrial production and quality control of monoester alkaloids from Radix Aconiti Preparata.展开更多
Antibodies targeting non-structural protein 1(NS1)confer protection against Zika virus(ZIKV).Although monoclonal an-tibodies(MAbs)3G2 and 4B8 are more potent than MAb 4F10 in suppressing ZIKV infection in neonatal mic...Antibodies targeting non-structural protein 1(NS1)confer protection against Zika virus(ZIKV).Although monoclonal an-tibodies(MAbs)3G2 and 4B8 are more potent than MAb 4F10 in suppressing ZIKV infection in neonatal mice models,the epitopes are unclear.Herein,we determined the Cryo-electron microscopy(Cryo-EM)structures of ZIKV NS1 in com-plex withfive human antibodies at 2.6–2.9Åresolution.Group I antibodies(3G2 and 4B8)recognize the previously un-reported epitopes on the outer surface of the NS1 dimer.The unique binding mode of Group I antibodies led to a stronger recognition of the cell surface form of NS1 and completely inhibited secreted form non-structural protein 1(sNS1)-induced endothelial permeability via their immunoglobulin G(IgG)and Fab.Group II antibodies(4F10,2E11,and 14G5)recognize common epitopes in the distal end of the b-ladder domain,with a blockade efficiency that may be related to their affinity for the sNS1 protein and the presence of full-length IgG.Thesefindings elucidate the correlation between epitope recognition and protective efficacy of anti-NS1 antibodies and highlight the diagnostic and therapeutic potential of 3G2 and 4B8.展开更多
基金Supported by Traditional Chinese Medicine Science and Technology Development Program of Shandong Province (2017-1982019-0400)Major Science and Technology Innovation Project of Shandong Province (2018CXGC1304)。
文摘[Objectives] This study was conducted to optimize the ethanol extraction technology of monoester alkaloids from Radix Aconiti Preparata. [Methods]On the basis of defined extraction times,ethanol concentration,ethanol times and extraction time were investigated by HPLC-MS combined with orthogonal test to optimize extraction process using the content of monoester alkaloids( the sum of benzoyl neoaconitine,benzoyl hypoaconitine and benzoyl aconitine) as an index.[Results]The optimum ethanol extraction technology was as follows: 75% ethanol,ethanol amount 25 times of the medicinal material,and each extraction for 1. 5 h.[Conclusions] The optimal extraction technology is simple,feasible,stable and reliable. It can provide reference for the industrial production and quality control of monoester alkaloids from Radix Aconiti Preparata.
基金supported by grants from the National Natural Science Foundation of China(81971924 to L.Y.and 32370146 to W.Z.)Guangzhou Municipal Science and Technology Bureau(2023A03J0791 to L.Y.)+6 种基金Guangdong Science and Technology Program(2021B1212030014 to W.Z.)Guangdong Basic and Applied Basic Research Fund Enterprise Joint Fund(2021A1515220017 to W.Z.)Medical Scientific Research Foundation of Guangdong Province(B2022112 to J.Y.),Shenzhen Science and Technology Innovation Committee(JCYJ20210324131802008 to H.H.)Ganghong Young Scholar Development Fund(to H.H.)the Shenzhen-Hong Kong Cooperation Zone for Technology and Innovation(HZQB-KCZYB-2020056 to H.H.)the Kobilka Institute of Innovative Drug Discovery and Presidential Fellowship and University Development Fund at the Chinese University of Hong Kong,Shenzhen(to H.H.,H.J.,and Q.C.)Presidential Fellowship at the Chinese University of Hong Kong,Shenzhen(to Q.P.and W.Z.)。
文摘Antibodies targeting non-structural protein 1(NS1)confer protection against Zika virus(ZIKV).Although monoclonal an-tibodies(MAbs)3G2 and 4B8 are more potent than MAb 4F10 in suppressing ZIKV infection in neonatal mice models,the epitopes are unclear.Herein,we determined the Cryo-electron microscopy(Cryo-EM)structures of ZIKV NS1 in com-plex withfive human antibodies at 2.6–2.9Åresolution.Group I antibodies(3G2 and 4B8)recognize the previously un-reported epitopes on the outer surface of the NS1 dimer.The unique binding mode of Group I antibodies led to a stronger recognition of the cell surface form of NS1 and completely inhibited secreted form non-structural protein 1(sNS1)-induced endothelial permeability via their immunoglobulin G(IgG)and Fab.Group II antibodies(4F10,2E11,and 14G5)recognize common epitopes in the distal end of the b-ladder domain,with a blockade efficiency that may be related to their affinity for the sNS1 protein and the presence of full-length IgG.Thesefindings elucidate the correlation between epitope recognition and protective efficacy of anti-NS1 antibodies and highlight the diagnostic and therapeutic potential of 3G2 and 4B8.
