Study on the antibacterial activities of emodin derivatives against clinical drug-resistant bacterial strains and their interaction with proteins.

ABSTRACT:

Background

Novel haloemodin (HEI2) synthesized by modifying emodin, a traditional Chinese medicine component, possesses remarkable antibacterial activity, being much more effective than its parent nucleus, emodin.

Methods

Firstly, we discovered that HEI2 increases bacterial cell membrane permeability to potassium ions more drastically than emodin. We thus further investigated the interaction of haloemodin and protein using a fluorescence quenching and circular dichroism (CD) study based on bovine serum albumin (BSA).

Results

HEI2 spontaneously bound to BSA at Trp 212 residue (subdomain IIA) by hydrogen bonds and van der Waals interactions to forms HEI2-BSA complexes, and this binding decreased the α-helical content of BSA. We also confirmed that emodin bound to BSA by

SUBMITTER: Ji C 

PROVIDER: S-EPMC7049003 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature