Electrochemical Late‐Stage Stitching of Tryptophan Peptides via N─S Bond Formation

X Xinwei Hu (Department of Guangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology and the State Key Laboratory of Respiratory Disease School of Pharmaceutical Sciences Guangzhou Medical University Guangzhou 511436 P.R. China) Z Zaimu Cao (Department of Guangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology and the State Key Laboratory of Respiratory Disease School of Pharmaceutical Sciences Guangzhou Medical University Guangzhou 511436 P.R. China) M Mu Chen C Chun‐Dong Huang (College of Chemistry & Chemical Engineering and Key Laboratory For Preparation and Application of Ordered Structural Materials of Guangdong Province Shantou University Shantou China) S Shao‐Fei Ni (College of Chemistry & Chemical Engineering and Key Laboratory For Preparation and Application of Ordered Structural Materials of Guangdong Province Shantou University Shantou China) S Shou‐Kun Zhang (Department of Guangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology and the State Key Laboratory of Respiratory Disease School of Pharmaceutical Sciences Guangzhou Medical University Guangzhou 511436 P.R. China) Z Zhixiong Ruan (Department of Guangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology and the State Key Laboratory of Respiratory Disease School of Pharmaceutical Sciences Guangzhou Medical University Guangzhou 511436 P.R. China)

Abstract

Abstract Late‐stage diversification of peptides via selective modification of endogenous amino acid side chains provides a powerful strategy to access analogues with enhanced bioactivity and tailored physicochemical properties, thereby facilitating peptide‐based drug discovery. However, precise manipulation of short peptides comprising canonical amino acids—particularly control over backbone conformation—remains a formidable challenge. Herein, we present a robust electrochemical strategy for constructing macrocyclic peptides through direct incorporation of diverse aryl sulfur linkers. This method enables tryptophan (Trp)‐selective crosslinking via electrochemical reaction with aryl thiosulfonates, leading to efficient formation of S─N bonds. The resulting sulfur‐bridged multi‐aryl macrocycles act as conformationally adaptive scaffolds that reshape the peptide backbone architecture. This conformational remodeling grants access to previously inaccessible structural spaces that are critical for modulating biological activity.

Article Details

Volume / Issue Vol. 64, Issue 49
Published December 01, 2025
ISSN 1433-7851
Publisher Wiley

Journal Info

Angewandte Chemie International Edition

Wiley

ISSN: 1433-7851 Physical Sciences

Authors (7)

X

Xinwei Hu

Department of Guangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology and the State Key Laboratory of Respiratory Disease School of Pharmaceutical Sciences Guangzhou Medical University Guangzhou 511436 P.R. China

Z

Zaimu Cao

Department of Guangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology and the State Key Laboratory of Respiratory Disease School of Pharmaceutical Sciences Guangzhou Medical University Guangzhou 511436 P.R. China

M

Mu Chen

C

Chun‐Dong Huang

College of Chemistry & Chemical Engineering and Key Laboratory For Preparation and Application of Ordered Structural Materials of Guangdong Province Shantou University Shantou China

S

Shao‐Fei Ni

College of Chemistry & Chemical Engineering and Key Laboratory For Preparation and Application of Ordered Structural Materials of Guangdong Province Shantou University Shantou China

S

Shou‐Kun Zhang

Department of Guangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology and the State Key Laboratory of Respiratory Disease School of Pharmaceutical Sciences Guangzhou Medical University Guangzhou 511436 P.R. China

Z

Zhixiong Ruan

Department of Guangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology and the State Key Laboratory of Respiratory Disease School of Pharmaceutical Sciences Guangzhou Medical University Guangzhou 511436 P.R. China