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Table of Contents
Vol. 1, No. 3, 2009
Issue release date: April 2009
Section title: Research Article
J Innate Immun 2009;1:268–280
(DOI:10.1159/000174822)

The Central Kink Region of Fowlicidin-2, an α-Helical Host Defense Peptide, Is Critically Involved in Bacterial Killing and Endotoxin Neutralization

Xiao Y.a · Herrera A.I.c · Bommineni Y.R.a · Soulages J.L.b · Prakash O.c · Zhang G.a
Departments of aAnimal Science and bBiochemistry and Molecular Biology, Oklahoma State University, Stillwater, Okla., and cDepartment of Biochemistry, Kansas State University, Manhattan, Kans., USA

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Article / Publication Details

First-Page Preview
Abstract of Research Article

Received: July 17, 2008
Accepted: September 29, 2008
Published online: November 14, 2008
Issue release date: April 2009

Number of Print Pages: 13
Number of Figures: 7
Number of Tables: 2

ISSN: 1662-811X (Print)
eISSN: 1662-8128 (Online)

For additional information: http://www.karger.com/JIN

Abstract

Fowlicidins are a group of newly identified chicken cathelicidin host defense peptides. We have shown that the putatively mature fowlicidin-2 of 31 amino acid residues possesses potent antibacterial and lipopolysaccharide (LPS)- neutralizing activities, but with a noticeable toxicity to mammalian cells. As a first step in exploring the structure-activity relationships of fowlicidin-2, in this study we determined its tertiary structure by nuclear magnetic resonance spectroscopy. Unlike the majority of cathelicidins, which are composed of a predominant α-helix with a short hinge sequence near the center, fowlicidin-2 consists of 2 well-defined α-helical segments (residues 6–12 and 23–27) connected by a long extensive kink (residues 13–20) induced by proline. To further investigate the functional significance of each of these structural components, several N- and C-terminal deletion analogs of fowlicidin-2 were synthesized and analyzed for their antibacterial, cytotoxic and LPS-neutralizing activities. Our results indicated that neither the N- nor C-terminal α-helix alone is sufficient to confer any function. Rather, fowlicidin-2(1–18) and fowlicidin-2(15–31), 2 α-helical segments with inclusion of the central cationic kink region, retained substantial capacities to kill bacteria and neutralize the LPS-induced proinflammatory response, relative to the parent peptide. More desirably, these 2 peptide analogs showed substantially reduced toxicity to human erythrocytes and epithelial cells, indicative of improved potential as antibacterial and antisepsis agents. To our knowledge, fowlicidin-2 is the first α-helical cathelicidin, with the central kink region shown to be critically important in killing bacteria and neutralizing LPS.

© 2008 S. Karger AG, Basel


Article / Publication Details

First-Page Preview
Abstract of Research Article

Received: July 17, 2008
Accepted: September 29, 2008
Published online: November 14, 2008
Issue release date: April 2009

Number of Print Pages: 13
Number of Figures: 7
Number of Tables: 2

ISSN: 1662-811X (Print)
eISSN: 1662-8128 (Online)

For additional information: http://www.karger.com/JIN


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Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
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