Skip Navigation


Bioinformatics Advance Access originally published online on February 5, 2004
This Article
Right arrow FREE Full Text (Print PDF) Freely available
Right arrow FREE Full Text (Screen PDF)
Right arrow All Versions of this Article:
20/6/970    most recent
bth027v1
Right arrow Comments: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when Comments are posted
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 ISI Web of Science
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 Search for citing articles in:
ISI Web of Science (2)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Han, X.
Right arrow Articles by Kang, W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Han, X.
Right arrow Articles by Kang, W.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Bioinformatics 20(6) © Oxford University Press 2004; all rights reserved.

Sequence analysis and membrane partitioning energies of {alpha}-helical antimicrobial peptides

Xing Han * and Wenjun Kang {dagger}

DuPont Haskell Laboratory for Health and Environmental Sciences, P.O. Box 50, Newark, DE 19714, USA

Received on August 5, 2003 ; revised on November 2, 2003 ; accepted on November 10, 2003
Advance Access Publication February 5, 2004

Sequences of 221 {alpha}-helical antimicrobial peptides ({alpha}AMPs) were compared and 63–166 of them were selected and analyzed using Perl programs. The results showed that aliphatic amino acids Gly, Leu, Ala, Ile and two positively charged amino acids Lys and Arg were composed of more than 63% of the first 20 residues of {alpha}AMPs. The weighed mean membrane partitioning energies at positions from 1 to 25 of {alpha}AMPs were calculated. Profile of the partitioning energies suggests oblique membrane insertion and an amphipathic {alpha}-helical structure of the N-terminus of {alpha}AMP (residues from 1 to 13), a bend structure at positions 13 and 14, and a less structured C-terminus that parallels the surface of the membrane. These structural features are in good agreement with the experimentally determined membrane structure of hemagglutinin fusion peptide from influenza virus. We hypothesize that this (N-terminal oblique {alpha}-helix)—central bend—(C-terminus) could be a common structural motif of membrane-disruptive peptides.

Contact: xing.han{at}usa.dupont.com

* To whom correspondence should be addressed.

{dagger} Present address: University of Minnesota School of Dentistry, 515 Delaware ST. SE, RM 6-320, Minneapolis, MN 55455, USA.


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


This article has been cited by other articles:


Home page
 FASEB J.Home page
B. Gao, P. Sherman, L. Luo, J. Bowie, and S. Zhu
Structural and functional characterization of two genetically related meucin peptides highlights evolutionary divergence and convergence in antimicrobial peptides
FASEB J, April 1, 2009; 23(4): 1230 - 1245.
[Abstract] [Full Text] [PDF]


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.