2000年9月
Gene-engineered hydrophobilization to alter the bactericidal activity of lysozyme
JOURNAL OF BIOACTIVE AND COMPATIBLE POLYMERS
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- 巻
- 15
- 号
- 5
- 開始ページ
- 376
- 終了ページ
- 395
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1106/Q11W-F3ED-U05C-4GUR
- 出版者・発行元
- TECHNOMIC PUBL CO INC
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.
- リンク情報
- ID情報
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- DOI : 10.1106/Q11W-F3ED-U05C-4GUR
- ISSN : 0883-9115
- J-Global ID : 200902100428715868
- Web of Science ID : WOS:000089450100002