Synthetically modified L-histidine-rich peptidomimetics exhibit potent activity against Cryptococcus neoformans.

ABSTRACT: We describe the synthesis and antimicrobial evaluation of structurally new peptidomimetics, rich in synthetically modified L-histidine. Two series of tripeptidomimetics were synthesized by varying lipophilicity at the C-2 position of L-histidine and at the N- and C-terminus. The data indicates that peptides (5f, 6f, 9f and 10f) possessing highly lipophilic adamantan-1-yl group displayed strong inhibition of Cryptococcus neoformans. Peptide 6f is the most potent of all with IC50 and MFC values of 0.60 and 0.63 μg/mL, respectively, compared to the commercial drug amphotericin B (IC50=0.69 and MFC=1.25 μg/mL). The selectivity of these peptides to microbial pathogen was examined by a tryptophan fluorescence quenching study and transmission electron microscopy. These studies indicate that the p

SUBMITTER: Mahindra A 

PROVIDER: S-EPMC4065882 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature