본문으로 건너뛰기
← 뒤로

A one-step, resin-compatible Cys-Trp cross-linking system opens a new avenue for stapled peptide therapeutics.

2/5 보강
Bioorganic & medicinal chemistry 📖 저널 OA 4% 2024: 0/3 OA 2025: 0/27 OA 2026: 3/43 OA 2024~2026 2026 Vol.137() p. 118622 Chemical Synthesis and Analysis
Retraction 확인
출처
PubMed DOI OpenAlex 마지막 보강 2026-04-28
OpenAlex 토픽 · Chemical Synthesis and Analysis Click Chemistry and Applications Sulfur-Based Synthesis Techniques

Denda M, Kohmura Y, Kobayashi D, Yoshimaru T, Fukuda S, Ando H, Ishida T, Katagiri T, Otaka A

📝 환자 설명용 한 줄

Protein-protein interactions (PPIs) are attractive yet challenging drug targets, motivating the development of conformationally constrained peptides such as stapled α-helices.

이 논문을 인용하기

↓ .bib ↓ .ris
APA Masaya Denda, Yutaka Kohmura, et al. (2026). A one-step, resin-compatible Cys-Trp cross-linking system opens a new avenue for stapled peptide therapeutics.. Bioorganic & medicinal chemistry, 137, 118622. https://doi.org/10.1016/j.bmc.2026.118622
MLA Masaya Denda, et al.. "A one-step, resin-compatible Cys-Trp cross-linking system opens a new avenue for stapled peptide therapeutics.." Bioorganic & medicinal chemistry, vol. 137, 2026, pp. 118622.
PMID 41818855 ↗

Abstract

Protein-protein interactions (PPIs) are attractive yet challenging drug targets, motivating the development of conformationally constrained peptides such as stapled α-helices. Here we report a one-pot cysteine-tryptophan (Cys-Trp) cross-linking strategy that enables direct formation of Trp-indole CH sulfenylation staples concomitant with global side-chain deprotection and resin cleavage. Application of this approach afforded a Cys-Trp-stapled analogue of estrogen receptor-α (ERα) activity regulator synthetic peptide (ERAP), designed to disrupt a pathogenic PPI implicated in breast cancer. The resulting stapled ERAP, stERAP(C-W), exhibited potent and sustained antiproliferative activity comparable to that of the original stERAP. Moreover, stereochemical modification at the stapling residues was readily achieved, and circular dichroism (CD) analyses revealed a systematic decrease in α-helicity upon D-amino acid substitution. Overall, this study establishes Cys-Trp stapling as a concise and versatile platform for generating bioactive stapled peptides with tunable conformational properties.

🏷️ 키워드 / MeSH 📖 같은 키워드 OA만

🏷️ 같은 키워드 · 무료전문 — 이 논문 MeSH/keyword 기반