Journal Article

Modification of Antimicrobial Peptide with Low Molar Mass Poly(ethylene glycol)

Genghui Zhang, Baozhong Han, Xiaoyan Lin, Xin Wu and Husheng Yan

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 144, issue 6, pages 781-788
Published in print December 2008 | ISSN: 0021-924X
Published online October 2008 | e-ISSN: 1756-2651 | DOI: http://dx.doi.org/10.1093/jb/mvn134
Modification of Antimicrobial Peptide with Low Molar Mass Poly(ethylene glycol)

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PEGylation of peptide drugs prolongs their circulating lifetimes in plasma. However, PEGylation can produce a decrease in the in vitro bioactivity. Longer poly(ethylene glycol) (PEG) chains are favourable for circulating lifetimes but unfavourable for in vitro bioactivities. In order to circumvent the conflicting effects of PEG length, a hydrophobic peptide, using an antimicrobial peptide as a model, was PEGylated with short PEG chains. The PEGylated peptides self-assembled in aqueous solution into micelles with PEG shell and peptide core. In these micelles, the core peptides were protected by the shell, thus reducing proteolytic degradation. Meanwhile, most of the in vitro antimicrobial activities still remained due to the short PEG chain attached. The stabilities of the PEGylated peptides were much higher than that of the unPEGylated peptides in the presence of chymotrypsin and serum. The antimicrobial activities of the PEGylated peptides in the presence of serum, an ex vivo assay, were much higher than that of the unPEGylated peptide.

Keywords: antimicrobial peptides; micelles; PEGylation; peptides; self-assembly

Journal Article.  4402 words.  Illustrated.

Subjects: Biochemistry

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