Reaction of Chloroacetyl-Modified Peptides with Mercaptoundecahydrododecaborate (BSH) Is Accelerated by Basic Amino Acid Residues in the Peptide

Mizuki Kitamatsu, Ken Inoue, Naoki Yamagata, Hiroyuki Michiue

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

We assessed a reactivity of chloroacetyl-modified tripeptides consisting of various amino acid residues (Cl-3X) and mercaptoundecahydrododecaborate (BSH) by converting Cl-3X to its reactant (BS-3X). We showed that the Cl-3X consisting of basic amino acid residues (e.g., Arg) reacted with BSH effectively and its conversion decreased as the number of Arg residues in the Cl-3X decreased. Furthermore, a reactivity of the peptides with introduction of an alkyl linker between the triarginine and the chloroacetyl group (Cl-Cn-3R) with BSH decreased with increasing alkyl linker length. These results indicate that an electrostatic attraction of positively charged amino acid residues in the tripeptides and negatively charged BSH causes BSH to gather in a vicinity of the chloroacetyl group, resulting in an accelerated reaction. This work should aid a development of new boron agents using BSH in boron neutron capture therapy.

Original languageEnglish
Article number2200
JournalProcesses
Volume10
Issue number11
DOIs
Publication statusPublished - Nov 2022

Keywords

  • boron neutron capture therapy (BNCT)
  • BSH
  • peptide

ASJC Scopus subject areas

  • Bioengineering
  • Chemical Engineering (miscellaneous)
  • Process Chemistry and Technology

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