Diaminodiacid bridge improves enzymatic and in vivo inhibitory activity of peptide CPI-1 against botulinum toxin serotype A

The replacement of a disulfide bridge by diaminodiacid bridge significantly improves enzymatic and in vivo inhibitory activity of peptide CPI-1 against botulinum toxin serotype A, the addition of hydrophobic or positive amino acid at C-terminus of modified peptides further improves the inhibitory ac...

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Bibliographic Details
Published in:Chinese chemical letters 2021-12, Vol.32 (12), p.4049-4052
Main Authors: Shen, Jintao, Liu, Jia, Yu, Shuo, Yu, Yunzhou, Huang, Chao, Xiong, Xianghua, Yue, Junjie, Dai, Qiuyun
Format: Article
Language:English
Subjects:
Botulinum neurotoxin serotype A
Diaminodiacid bridges
Inhibitory activity
Light chain inhibitor
Peptide CPI-1
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Summary:The replacement of a disulfide bridge by diaminodiacid bridge significantly improves enzymatic and in vivo inhibitory activity of peptide CPI-1 against botulinum toxin serotype A, the addition of hydrophobic or positive amino acid at C-terminus of modified peptides further improves the inhibitory activity. [Display omitted] 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.
ISSN:1001-8417
1878-5964
DOI:10.1016/j.cclet.2021.03.055