Related Experiment Video
Updated: May 23, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
Published on: August 1, 2018
Inter-chain acyl transfer reaction in a peptide six-helical bundle: a chemical method for regulating the interaction
Yu Bai1, Huifang Xue, Yanbo Ling
1Beijing Institute of Pharmacology and Toxicology, 27 Taiping Road, Haidian District, Beijing 100850, China.
Abstract:
An inter-helical acyl transfer specifically occurred between the C-and N-peptides of HIV gp41 after assembly of the six-helical bundle (6HB), forming an inter-helical covalent bond that greatly enhanced 6HB stability. In the reaction, the C-peptide was modified as an acyl donor, and the N-peptide served as an acyl acceptor.
Related Concept Videos
Peptide Bonds
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Phase II Reactions: Acetylation Reactions
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Protein Organization
The primary structure of a protein is its amino acid sequence.

