Interactions between HIV-1 protease, silver nanoparticles, and specific peptides

被引:14
作者
Tsai, Chieh-Hsuan [1 ]
Whiteley, Chris G. [2 ]
Lee, Duu-Jong [1 ,3 ,4 ,5 ]
机构
[1] Natl Taiwan Univ, Dept Chem Engn, Taipei 10617, Taiwan
[2] Rhodes Univ, Dept Biochem & Microbiol, Grahamstown, South Africa
[3] Natl Taiwan Univ Sci & Technol, Dept Chem Engn, Taipei 10607, Taiwan
[4] Tunghai Univ, Coll Engn, Taichung 40704, Taiwan
[5] Natl Taiwan Normal Univ, Coll Technol & Engn, Taipei 10610, Taiwan
关键词
Silver nanoparticles; HIV-1; protease; Inhibition; Cleavage; HUMAN-IMMUNODEFICIENCY-VIRUS; ACTIVE-SITE; SUBSITE PREFERENCES; PROTEINASE; INHIBITORS; SUBSTRATE;
D O I
10.1016/j.jtice.2019.07.019
中图分类号
TQ [化学工业];
学科分类号
0817 ;
摘要
Use of silver nanoparticles (Ag NP's) as inhibitor for HIV-1 protease (PR) has practical interest. However, the interactions between the Ag NP's, HIV-1 PR, and the target peptides are not well demonstrated. This study experimentally revealed the interactions of the synthesized Ag NP's, HIV-1 PR, and five specific peptides with similar amino acid sequences to HIV's polyproteins. The Ag NP's can bind with either HIV-1 PR or the peptides. Incubating Ag NP's with peptide for 24 h can efficiently inhibit activity of HIV-1 PR. But HIV-1 PR would cleave peptides faster than the binding rate of Ag NP's and the peptides; therefore, late presence of Ag NP's would have no inhibition on the HIV-1 PR activity. (C) 2019 Taiwan Institute of Chemical Engineers. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:20 / 32
页数:13
相关论文
共 28 条
[1]   ANALYSIS OF SUBSITE PREFERENCES OF HIV-1 PROTEINASE USING MA/CA JUNCTION PEPTIDES SUBSTITUTED AT THE P3-P1' POSITIONS [J].
BILLICH, A ;
WINKLER, G .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1991, 290 (01) :186-190
[2]  
Calles NR, 2006, PATHOPHYSIOLOGY HUMA
[3]   The inhibitory effects of silver nanoparticles, silver ions, and silver chloride colloids on microbial growth [J].
Choi, Okkyoung ;
Deng, Kathy Kanjun ;
Kim, Nam-Jung ;
Ross, Louis, Jr. ;
Surampalli, Rao Y. ;
Hu, Zhiqiang .
WATER RESEARCH, 2008, 42 (12) :3066-3074
[4]   Enhanced Antibacterial Activity of Bifunctional Fe3O4-Ag Core-Shell Nanostructures [J].
Chudasama, Bhupendra ;
Vala, Anjana K. ;
Andhariya, Nidhi ;
Upadhyay, R. V. ;
Mehta, R. V. .
NANO RESEARCH, 2009, 2 (12) :955-965
[5]  
Elechiguerra Jose Luis, 2005, J Nanobiotechnology, V3, P6
[6]   HIV-1 TAT TRANS-ACTIVATION REQUIRES THE LOOP SEQUENCE WITHIN TAR [J].
FENG, S ;
HOLLAND, EC .
NATURE, 1988, 334 (6178) :165-167
[7]   FINE-STRUCTURE OF HUMAN-IMMUNODEFICIENCY-VIRUS (HIV) AND IMMUNOLOCALIZATION OF STRUCTURAL PROTEINS [J].
GELDERBLOM, HR ;
HAUSMANN, EHS ;
OZEL, M ;
PAULI, G ;
KOCH, MA .
VIROLOGY, 1987, 156 (01) :171-176
[8]   Comparison of HIV-1 and HIV-2 infectivity from a prospective cohort study in Senegal [J].
Gilbert, PB ;
McKeague, IW ;
Eisen, G ;
Mullins, C ;
Guéye-NDiaye, A ;
Mboup, S ;
Kanki, PJ .
STATISTICS IN MEDICINE, 2003, 22 (04) :573-593
[9]   DIFFERENT REQUIREMENTS FOR PRODUCTIVE INTERACTION BETWEEN THE ACTIVE-SITE OF HIV-1 PROTEINASE AND SUBSTRATES CONTAINING -HYDROPHOBIC-ASTERISK HYDROPHOBIC- OR -AROMATIC-ASTERISK PRO- CLEAVAGE SITES [J].
GRIFFITHS, JT ;
PHYLIP, LH ;
KONVALINKA, J ;
STROP, P ;
GUSTCHINA, A ;
WLODAWER, A ;
DAVENPORT, RJ ;
BRIGGS, R ;
DUNN, BM ;
KAY, J .
BIOCHEMISTRY, 1992, 31 (22) :5193-5200
[10]   CHARACTERIZATION OF RIBOSOMAL FRAMESHIFTING IN HIV-1 GAG-POL EXPRESSION [J].
JACKS, T ;
POWER, MD ;
MASIARZ, FR ;
LUCIW, PA ;
BARR, PJ ;
VARMUS, HE .
NATURE, 1988, 331 (6153) :280-283