TAILIEUCHUNG - Báo cáo khoa học: The capsid protein of human immunodeficiency virus: designing inhibitors of capsid assembly

The mature capsid of human immunodeficiency virus, HIV-1, is formed by the assembly of copies of a capsid protein (CA). The C-terminal domain of CA, CTD, is able to homodimerize and most of the dimerization interface is formed by a single a-helix from each monomer. Assembly of the HIV-1 capsid critically depends on CA–CA interactions, including CTD interac-tion with itself and with the CA N-terminal domain, NTD. | MINIREVIEW The capsid protein of human immunodeficiency virus designing inhibitors of capsid assembly Jose L. Neira1 2 1 Institute de Biologia Molecular y Celular Universidad MiguelHernandez Alicante Spain 2 Biocomputation and Complex Systems Physics Institute Zaragoza Spain Keywords CTD protein HIV NMR organic molecules protein-peptide interactions protein-protein interactions structure X-ray crystallography Correspondence J. L. Neira Instituto de Biologia Molecular y Celular Edificio Torregaitan Universidad MiguelHernandez Avda. delFerrocarrils n 03202 Elche Alicante Spain Fax 34 9666 58758 Tel 34 9666 58459 E-mail jlneira@ Note The author would like to dedicate this paper to Professors ManuelRico and Alan Fersht for allowing him to learn beside them The mature capsid of human immunodeficiency virus HIV-1 is formed by the assembly of copies of a capsid protein CA . The C-terminal domain of CA CTD is able to homodimerize and most of the dimerization interface is formed by a single a-helix from each monomer. Assembly of the HIV-1 capsid critically depends on CA-CA interactions including CTD interaction with itself and with the CA N-terminal domain NTD. This minireview reports on the search and the design of peptides and small organic compounds that are able to interact with the CTD and or CA of HIV-1. Such molecules aim to disrupt and or alter the oligomerization capability of CTD. The different peptides designed so far interact with CTD mainly via hydrophobic contacts with residues close or belonging to the interface between the dimerization helices. A CTD-binding organic compound also establishes hydrophobic contacts with regions involved in the interface between the NTD and CTD. These results open new venues for the development of new antiviral drugs that are able to interact with CA and or its domains hampering HIV-1 assembly and infection. Received 9 February 2009 revised 2 July 2009 accepted 24 July 2009 doi Introduction

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