Structure-activity relationship study of the bacterial actin-like protein MreB inhibitors: effects of substitution of benzyl group in S-benzylisothiourea

Noritaka Iwai; Takuya Fujii; Hirokatsu Nagura; Masaaki Wachi; Tomoya Kitazume

doi:10.1271/bbb.60443

Structure-activity relationship study of the bacterial actin-like protein MreB inhibitors: effects of substitution of benzyl group in S-benzylisothiourea

Biosci Biotechnol Biochem. 2007 Jan;71(1):246-8. doi: 10.1271/bbb.60443. Epub 2007 Jan 7.

Authors

Noritaka Iwai¹, Takuya Fujii, Hirokatsu Nagura, Masaaki Wachi, Tomoya Kitazume

Affiliation

¹ Department of Bioengineering, Tokyo Institute of Technology, Japan. niwai@bio.titech.ac.jp

PMID: 17213642
DOI: 10.1271/bbb.60443

Abstract

We comprehensively investigated the effects of substitution of the benzyl group in S-benzylisothiourea derivatives on antibacterial activity, because we found previously that some substitutions enhanced it. A 2,4-Cl2-derivative was found to be the most effective compound, it was stronger than the original one in Gram-negative rod shaped-bacteria such as Escherichia coli and Salmonella typhimurium.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Actins / antagonists & inhibitors*
Actins / genetics
Actins / metabolism*
Bacterial Proteins / antagonists & inhibitors*
Bacterial Proteins / metabolism*
Escherichia coli / drug effects
Escherichia coli / metabolism
Molecular Structure
Salmonella typhimurium / drug effects
Salmonella typhimurium / metabolism
Structure-Activity Relationship
Thiourea* / analogs & derivatives
Thiourea* / chemistry
Thiourea* / pharmacology

Substances

Actins
Bacterial Proteins
Thiourea