This Article Full Text (PDF) References Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Add to Saved Citations Download to citation manager Request Permissions Request Reprints Add to My Marked Citations Citing Articles Citing Articles via Google Scholar Citing Articles via Scopus Google Scholar Articles by Ito, Y. Articles by Imanishi, Y. Search for Related Content Social Bookmarking                         What's this?

Gene-Engineered Hydrophobilization to Alter the Bactericidal Activity of Lysozyme

Department of Biological Science and Technology, Faculty of Engineering, The University of Tokushima, Tokushima 770-8506, Japan, ito{at}bio.tokushima-u.ac.jp

Oh Hyeong Kwon

Department of Material Chemistry, Graduate School of Engineering, Kyoto University, Kyoto 606-8758, Japan

Mitsuyoshi Ueda

Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto 606-8758, Japan

Atsuo Tanaka

Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto 606-8758, Japan

Yukio Imanishi

Graduate School of Materials Science, NAIST, Ikoma 630-0101, Japan

The hydrophobic polypeptide, polyproline, which has different chain lengths, was connected to the C-terminus of human lysozyme by recombinant DNA techniques. The hydrophobicity of human lysozyme increased with the increasing length of the polyproline chain. No significant perturbation of the secondary structure of lysozyme by incorporation of the polyproline chain was observed by circular dichroism spectroscopy. Although the bactericidal activity of wild-type human lysozyme is limited to Gram-positive bacteria (M. luteus and B. subtilis), the mutant lysozymes showed bactericidal activity to Gram-negative bacteria (E. coli and P. aeruginosa), and the activity increased with the increasing hydrophobicity of the mutant enzyme. Experiments with E. coli phospholipid liposomes revealed that the mutant lysozymes enhanced the release of the liposome contents, and this release increased with the increase of hydrophobicity. The increased hydrophobicity of the mutant enzyme may induce the interaction of lysozyme with the outer membrane E. coli and subsequent penetration into the inner membrane, resulting in the increase of bactericidal activity.

Journal of Bioactive and Compatible Polymers, Vol. 15, No. 5, 376-395 (2000)
DOI: 10.1106/Q11W-F3ED-U05C-4GUR


CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?