Journal
PROCESSES
Volume 10, Issue 11, Pages -Publisher
MDPI
DOI: 10.3390/pr10112200
Keywords
BSH; peptide; boron neutron capture therapy (BNCT)
Categories
Ask authors/readers for more resources
This study assessed the reactivity between chloroacetyl-modified tripeptides with different amino acid residues and mercaptoundecahydrododecaborate. The results showed that the reactivity varied with the type and number of amino acid residues as well as the length of the alkyl linker. The electrostatic attraction between positively charged amino acid residues and negatively charged mercaptoundecahydrododecaborate was found to play a key role in the accelerated reaction.
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available