Disulfide bond creates a small connecting loop in aminoxy peptide backbone.
Disulfide-bond formation between the side chains of cysteine-cysteine pairs is often critical to the folding behavior, stability, and functionality of proteins. In this paper, we report that sulfur atoms can be introduced into the amide groups of aminoxy peptides to form a novel type of disulfide bridge, which creates a connecting loop in the peptide backbone.
Yang
Dan
D
Department of Chemistry, Fudan University, Shanghai, China.
Liu
Guo-Jun
GJ
Jiao
Zhi-Gang
ZG
Zhang
Dan-Wei
DW
Luo
Zheng
Z
Song
Ke-Sheng
KS
Chen
Min-Qin
MQ
D000588:Amines / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D015394:Molecular Structure; D010087:Oxides / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D013053:Spectrophotometry; D013438:Sulfhydryl Compounds / Q000737:chemistry
D000588:Amines; D004220:Disulfides; D010087:Oxides; D010455:Peptides; D013438:Sulfhydryl Compounds