Issue 94, 2013
From the journal:

Chemical Communications

Exchangeability of amino acid residues with similar physicochemical properties in coiled-coil interactions†

Guiying Zhang,‡a   Kun Wang,‡ab   Baohua Zheng,‡ac   Maosheng Cheng,c   Yanni Li,*b   Keliang Liu*a  and  Lifeng Cai*a  

* Corresponding authors

a Department of Medicinal Chemistry, Beijing Institute of Pharmacology & Toxicology, 27 Taiping Rd, Haidian District, Beijing 100850, China
E-mail: caileefeng@gmail.com, keliangliu55@126.com
Fax: +86-10-68211656

b Key Laboratory of Systems Bioengineering, Ministry of Education, Department of Pharmaceutical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China
E-mail: liyanni@tju.edu.cn

c Key Lab. Struc. Based Drug Design & Discovery, Ministry of Education, Shenyang Pharmaceutical University, Shenyang 110016, China

Abstract

Systematic exchange of amino acid residues of similar physicochemical properties maintains specific coiled-coil interaction between two heptad repeats of HIV-1 gp41, as well as the biological activity of related peptide fusion inhibitors. This exchangeability can greatly degenerate sequence space of peptides thus making ab initio design of coiled-coil interaction feasible.

Graphical abstract: Exchangeability of amino acid residues with similar physicochemical properties in coiled-coil interactions

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/C3CC46560H
Article type
Communication
Submitted
28 Aug 2013
Accepted
08 Oct 2013
First published
08 Oct 2013

Chem. Commun., 2013,49, 11086-11088

Permissions

Request permissions

Exchangeability of amino acid residues with similar physicochemical properties in coiled-coil interactions

G. Zhang, K. Wang, B. Zheng, M. Cheng, Y. Li, K. Liu and L. Cai, Chem. Commun., 2013, 49, 11086 DOI: 10.1039/C3CC46560H

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements