De novo design of constrained and sequence-independent peptide scaffolds with topologically-formidable disulfide connectivities-Reference-Cited by-同舟云学术

De novo design of constrained and sequence-independent peptide scaffolds with topologically-formidable disulfide connectivities

Published:2018 Issue:3 Volume:9 Page:569-575
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Zheng Yiwu¹²³⁴⁵,Meng Xiaoting¹²³⁴⁵,Wu Yaqi¹²³⁴⁵,Zhao Yibing¹²³⁴⁵,Wu Chuanliu¹²³⁴⁵^ORCID

Affiliation:

1. The MOE Key Laboratory of Spectrochemical Analysis and Instrumentation

2. State Key Laboratory of Physical Chemistry of Solid Surfaces

3. Department of Chemistry

4. College of Chemistry and Chemical Engineering

5. Xiamen University

Abstract

We developed a novel approach for designing a class of constrained and sequence-independent peptide scaffolds with three or four disulfide bonds. Even specific peptide folds that have been considered to be topologically formidable can be de novo created and synthesized in high yields.

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2018/SC/C7SC03956E

Reference38 articles.

1. Contemporary strategies for peptide macrocyclization

2. Constraining Cyclic Peptides To Mimic Protein Structure Motifs

3. Inhibition of α-helix-mediated protein–protein interactions using designed molecules