DStabilize: A Web Resource to Generate Mirror Images of Biomolecules
- PMID: 32783952
- DOI: 10.1016/j.str.2020.07.014
DStabilize: A Web Resource to Generate Mirror Images of Biomolecules
Erratum in
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DStabilize: A Web Resource to Generate Mirror Images of Biomolecules.Structure. 2020 Dec 1;28(12):1376-1378. doi: 10.1016/j.str.2020.11.010. Structure. 2020. PMID: 33264596 No abstract available.
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.
Keywords: D-proteins; enantiomers; peptide design; protein structure transformation; retero-inverso.
Copyright © 2020 Elsevier Ltd. All rights reserved.
Conflict of interest statement
Declaration of Interests C.S.V. is founder director of SiNOPSEE Therapeutics and Aplomex. C.S.V. and P.G.A.A. are part of a team in A(∗)STAR who have a joint patent application with MSD International (P53 activator peptidomimetic macrocycles. US patent application no. 62864531, filed June 2019. Patent pending); C.S.V. receives research funding for his group (in the Bioinformatics Institute, A(∗)STAR) from MSD International for work on peptides; A.J.M. and P.G.A.A. declare no competing interests.
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