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.
Department of Chemistry, Fudan University, Shanghai, China.
Dan
D
Yang
Guo-Jun
GJ
Liu
Zhi-Gang
ZG
Jiao
Dan-Wei
DW
Zhang
Zheng
Z
Luo
Ke-Sheng
KS
Song
Min-Qin
MQ
Chen
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