95656-90-9Relevant articles and documents
Diaminodiacid bridge improves enzymatic and in vivo inhibitory activity of peptide CPI-1 against botulinum toxin serotype A
Shen, Jintao,Liu, Jia,Yu, Shuo,Yu, Yunzhou,Huang, Chao,Xiong, Xianghua,Yue, Junjie,Dai, Qiuyun
, p. 4049 - 4052 (2021)
The replacement of the disulfide bridge of CPI-1, a peptide inhibitor of light chain of Botulinum toxin serotype A, with the thioether-containing and biscarba-containing diaminodiacid bridge leads to a significant decrease in the degradation by trypsin and increase in the detoxification activity in vivo, the addition of hydrophobic or positive amino acid at C-terminus of modified peptides further improves the inhibitory activity.
MANIPULATION OF THE CARBOXYL GROUPS OF α-AMINO-ACIDS AND PEPTIDES USING RADICAL CHEMISTRY BASED ON ESTERS OF N-HYDROXY-2-THIOPYRIDONE
Barton, Derek H. R.,Herve, Yolande,Potier, Pierre,Thierry, Josiane
, p. 5479 - 5486 (2007/10/02)
Photolysis of α-amino-acid or peptide esters derived from N-hydroxy-2-thiopyridone in the presence of t-butylthiol affords the expected decarboxylation products in good yield.The reaction can be applied to the α-carboxyl or to the side chain carboxyl of g