Back to Search Start Over

DStabilize: A Web Resource to Generate Mirror Images of Biomolecules.

Authors :
Malik, Ashar J.
Aronica, Pietro G.A.
Verma, Chandra S.
Source :
Structure. Dec2020, Vol. 28 Issue 12, p1358-1358. 1p.
Publication Year :
2020

Abstract

Peptides comprising D-amino acids have been shown to be resistant to proteolysis. This makes them potential candidates as probes of cellular interactions, notably protein-biomolecule interactions. However, the empirical conversion of the amino acids that constitute a peptide from L-forms to D-forms will result in abrogation of the normal interactions made by the L-amino acids due to side-chain orientation changes that are associated with the changes in chirality. These interactions can be preserved by reversing the sequence of the D-peptide. We present a web server (http://dstabilize.bii.a-star.edu.sg/) that allows users to convert between L-proteins and D-proteins and for sequence reversal of D-peptides, along with the capability of performing other empirical geometric transforms. This resource allows the user to generate structures of interest easily for subsequent in silico processing. • Convert between L- and D-forms of peptides/protein structures • Apply custom geometrical transforms to structures of peptides/proteins • Generate retro-inverso forms of peptides • Webserver is available at http://dstabilize.bii.a-star.edu.sg/ The importance of D-amino acid-containing peptides as therapeutics is increasingly being recognized. In this work, Malik et al. present a webserver allowing users to easily interconvert between L- and D-forms of peptides/protein structures, apply custom geometrical transforms, and generate retro-inverso forms of peptides for in silico investigations. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
09692126
Volume :
28
Issue :
12
Database :
Academic Search Index
Journal :
Structure
Publication Type :
Academic Journal
Accession number :
147153975
Full Text :
https://doi.org/10.1016/j.str.2020.07.014