Peptide Stapling through Site-Directed Conjugation of Triazine Moieties to the Tyrosine Residues of a Peptide

Zhang, Yue; Yin, Ruijuan; Jiang, Hao; Wang, Chaoming; Wang, Xiao; Wang, Dongping; Zhang, Kai; Yu, Rilei; Li, Xuechen; Jiang, Tao

doi:10.1021/acs.orglett.3c00499

Cited by 7 publications

(3 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Zhang et al developed a novel method for linking two tyrosines (Tyr) with 1,3,5-triazine-2chloride and amines as cyclization reagents (Scheme 7). 37 By applying this method to staple the RGD peptide (an Arg-Gly-Asp peptide), the integrin-targeting ability and plasma stability of the peptide were significantly improved.…”

Section: Glu-glu Staplingmentioning

confidence: 99%

Recent Advances in Metal-Free Peptide Stapling Strategies

Zhan,

Duan,

2024

Chem Bio Eng.

View full text Add to dashboard Cite

Protein–protein interactions (PPIs) pose challenges for intervention through small molecule drugs, protein drugs, and linear peptides due to inherent limitations such as inappropriate size, poor stability, and limited membrane penetrance. The emergence of stapled α-helical peptides presents a promising avenue as potential competitors for inhibiting PPIs, demonstrating enhanced structural stability and increased tolerance to proteolytic enzymes. This review aims to provide an overview of metal-free stapling strategies involving two identical natural amino acids, two different natural amino acids, non-natural amino acids, and multicomponent reactions. The primary objective is to delineate comprehensive peptide stapling approaches and foster innovative ideation among readers by accentuating methodologies published within the past five years and elucidating evolving trends in stapled peptides.

show abstract

Section: Glu-glu Staplingmentioning

confidence: 99%

Recent Advances in Metal-Free Peptide Stapling Strategies

Zhan,

Duan,

2024

Chem Bio Eng.

View full text Add to dashboard Cite

show abstract

“…Consequently, they can be employed for live cell labeling and comprehensive tyrosine mapping within living cells. Zhang et al (2023) developed a selective construction strategy for stapled peptides using chlorotriazine moiety and Tyr phenol hydroxyl group (Scheme 8). Stapled peptides are a method to improve the biological properties of peptides.…”

Section: Cms Of the Side Chains Of C4-ohmentioning

confidence: 99%

“…Zhang et al (2023) developed a selective construction strategy for stapled peptides using chlorotriazine moiety and Tyr phenol hydroxyl group (Scheme 8). Stapled peptides are a method to improve the biological properties of peptides.…”

Section: Cms Of the Side Chains Of C4‐ohmentioning

confidence: 99%

Research progress on chemical modifications of tyrosine residues in peptides and proteins

Zeng,

Xue,

Geng

et al. 2023

Biotech & Bioengineering

View full text Add to dashboard Cite

The chemical modifications (CMs) of protein is an important technique in chemical biology, protein‐based therapy, and material science. In recent years, there has been rapid advances in the development of CMs of peptides and proteins, providing new approaches for peptide and protein functionalization, as well as drug discovery. In this review, we highlight the methods for chemically modifying tyrosine (Tyr) residues in different regions, offering a comprehensive exposition of the research content related to Tyr modification. This review summarizes and provides an outlook on Tyr residue modification, aiming to offer readers assistance in the site‐selective modification of macromolecules and to facilitate application research in this field.

show abstract

Peptide Stapling by Crosslinking Two Amines with α‐Ketoaldehydes through Diverse Modified Glyoxal‐Lysine Dimer Linkers

Guo,

Chu,

et al. 2024

Angewandte Chemie

View full text Add to dashboard Cite

α‐Ketoaldehydes play versatile roles in the ubiquitous natural processes of protein glycation. However, leveraging the reactivity of α‐ketoaldehydes for biomedical applications has been challenging. Previously, the reactivity of α‐ketoaldehydes with guanidine has been harnessed to design probes for labeling Arg residues on proteins in an aqueous medium. Herein, a highly effective, broadly applicable, and operationally simple protocol for stapling native peptides by crosslinking two amino groups through diverse imidazolium linkers with various α‐ketoaldehyde reagents is described. The use of hexafluoroisopropanol as a solvent facilitates rapid and clean reactions under mild conditions and enables unique selectivity for Lys over Arg. The naturally occurring GOLD/MOLD linkers have been expanded to encompass a wide range of modified glyoxal‐lysine dimer (OLD) linkers. In a proof‐of‐concept trial, these modular stapling reactions enabled a convenient two‐round strategy to streamline the structure‐activity relationship (SAR) study of the wasp venom peptide anoplin, leading to enhanced biological activities.

show abstract

Peptide Stapling through Site-Directed Conjugation of Triazine Moieties to the Tyrosine Residues of a Peptide

Cited by 7 publications

References 25 publications

Recent Advances in Metal-Free Peptide Stapling Strategies

Recent Advances in Metal-Free Peptide Stapling Strategies

Research progress on chemical modifications of tyrosine residues in peptides and proteins

Peptide Stapling by Crosslinking Two Amines with α‐Ketoaldehydes through Diverse Modified Glyoxal‐Lysine Dimer Linkers

Contact Info

Product

Resources

About