Stereoisomerism of stapled peptide inhibitors of the p53-Mdm2 interaction: an assessment of synthetic strategies and activity profiles-Reference-Cited by-同舟云学术

Stereoisomerism of stapled peptide inhibitors of the p53-Mdm2 interaction: an assessment of synthetic strategies and activity profiles

Published:2019 Issue:26 Volume:10 Page:6457-6466
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Yuen Tsz Ying¹²³⁴^ORCID,Brown Christopher J.⁵²³⁶,Xue Yuezhen⁵²³⁶,Tan Yaw Sing⁷²³⁸,Ferrer Gago Fernando J.⁵²³⁶,Lee Xue Er⁵²³⁶,Neo Jin Yong¹²³⁴,Thean Dawn⁵²³⁶,Kaan Hung Yi Kristal⁹⁴,Partridge Anthony W.⁹⁴^ORCID,Verma Chandra S.⁷²³⁸^ORCID,Lane David P.⁵²³⁶^ORCID,Johannes Charles W.¹²³⁴^ORCID

Affiliation:

1. Institute of Chemical and Engineering Sciences

2. Agency for Science

3. Technology and Research

4. Singapore 138665

5. P53 Laboratory

6. Singapore 138648

7. Bioinformatics Institute

8. Singapore 138671

9. MSD Translational Medicine Research Centre

Abstract

Staple composition can influence target binding and bioactivity of peptides. We present strategies to modulateE/Zratios and access saturated analogues.

Funder

Agency for Science, Technology and Research

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2019/SC/C9SC01456J

Reference71 articles.

1. General approach to the synthesis of short .alpha.-helical peptides

2. Synthesis of constrained helical peptides by thioether ligation: application to analogs of gp41

3. On-resin peptide macrocyclization using thiol–ene click chemistry