Comparative Conformational Analysis Of Peptide T Analogs
Abstract
A series of peptide T analogs were investigated within the molecular mechanics framework. In order to determine the role of the aminoacid residues in spatial formation of peptide T the conformational peculiarities of the glycine-substituted analogs were investigated. The conformational profiles of some biologically tested analogs of this peptide were determined independently. The received data permit to assess the active form of this peptide. It is characterized by p-turn at the C-terminal physiologically active pentapeptide fragment of peptide molecule. The received results are important for the investigation of the structure-activity relationship and may be used at design of a rigid-molecule drug against HIV. (c) 2008 Elsevier B.V. All rights reserved.
Subject
Peptide T Analogs
Conformational Analysis
Structure Activity Relationship
Immunodeficiency Virus Receptor
Hiv Infectivity
L-alanine
Binding
Pentapeptide
Ribonuclease
Inhibitor
Dynamics
Homology
GP120
Konformasyon Analizi
Yapı Aktivite İlişkisi
Bağışıklık Sistemi Bozucu Virüs Reseptörü
HIV Enfeksiyonu
Bağlayıcı
Ribonükleaz
Önleyici
Dinamik
Homoloji
Conformational Analysis
Structure Activity Relationship
Immunodeficiency Virus Receptor
Hiv Infectivity
L-alanine
Binding
Pentapeptide
Ribonuclease
Inhibitor
Dynamics
Homology
GP120
Konformasyon Analizi
Yapı Aktivite İlişkisi
Bağışıklık Sistemi Bozucu Virüs Reseptörü
HIV Enfeksiyonu
Bağlayıcı
Ribonükleaz
Önleyici
Dinamik
Homoloji
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