Title: The Hydrophobicity in a Chemically Modified Side-Chain of Cysteine Residues of Thanatin Is Related to Antimicrobial Activity against Micrococcus luteus.
Authors: Orikasa, Yoshitake; Ichinohe, Kenta; Saito, Junki; Hashimoto, Shigeki; Matsumoto, Ken'ichiro; Ooi, Toshihiko; Taguchi, Seiichi
Abstract: The article presents a study on the combination of the methyl group, ethyl group, and normal-octyl group at the side-chain of cysteine remains with the chemically transformed thanatins. The study shows that the octyl group modified form displays an 8-fold higher antimicrobial activity over Micrococcus luteus than the intense type thanatin. It concludes that an equilateral correlation exists between side-chain hydrophobicity and antimicrobial activity at the cysteine remains in thanatin.
Subjects: CYSTEINE proteinases; MICROCOCCUS luteus; CHEMICAL modification of proteins; PEPTIDE antibiotics; ANTI-infective agents
Publication: Bioscience, Biotechnology & Biochemistry, 2009, Vol 73, Issue 7, p1683
ISSN: 0916-8451
Publication type: Academic Journal
DOI: 10.1271/bbb.90183

The Hydrophobicity in a Chemically Modified Side-Chain of Cysteine Residues of Thanatin Is Related to Antimicrobial Activity against Micrococcus luteus.

Orikasa, Yoshitake; Ichinohe, Kenta; Saito, Junki; Hashimoto, Shigeki; Matsumoto, Ken'ichiro; Ooi, Toshihiko; Taguchi, Seiichi