Skip Navigation



Journal of Biochemistry Advance Access published online on October 9, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn134
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow Supplementary Data
Right arrow All Versions of this Article:
144/6/781    most recent
mvn134v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Zhang, G.
Right arrow Articles by Yan, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhang, G.
Right arrow Articles by Yan, H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2008 The Japanese Biochemical Society

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

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

Key Laboratory of Functional Polymer Materials (Nankai University), Ministry of Education; Institute of Polymer Chemistry, Nankai University, Tianjin 300071, P. R. China

*Corresponding author: Husheng Yan, Institute of Polymer Chemistry, Nankai University, Tianjin 300071, P. R. China. Tel: 86-22-25301705, Fax: 86-22-25303510, E-mail: yanhs{at}nankai.edu.cn

Received July 16, 2008; Accepted September 23, 2008


  Abstract

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 favorable for circulating lifetimes but unfavorable 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 peptide 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.

Key Words: antimicrobial peptides, micelles, PEGylation, peptides, self-assembly


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.