Structure-function relationships in the tryptophan-rich, antimicrobial peptide indolicidin

Indolicidin is a cationic 13 amino acid peptide amide produced in the granules of bovine neutrophils with the sequence H‐ILPWKWPWWPWRR‐NH2. Indolicidin is both antimicrobial and, to a lesser extent, haemolytic. In order to systematically investigate structure–function relationships, the solid‐phase...

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Bibliographic Details
Published in:Journal of peptide science 2001-10, Vol.7 (10), p.552-564
Main Authors: Staubitz, Petra, Peschel, Andreas, Nieuwenhuizen, Willem F., Otto, Michael, Götz, Friedrich, Jung, Günther, Jack, Ralph W.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Anti-Bacterial Agents - chemical synthesis
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - pharmacology
Antimicrobial Cationic Peptides - chemical synthesis
Antimicrobial Cationic Peptides - chemistry
Antimicrobial Cationic Peptides - pharmacology
antimicrobial peptide
Cattle
defence peptide
Escherichia coli - drug effects
Hemolysis - drug effects
Humans
In Vitro Techniques
indolicidin
indolicidin analogues
inverso-peptide
retro-peptide
Staphylococcus aureus - drug effects
Structure-Activity Relationship
structure-function relationships
Tryptophan - chemistry
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Summary:Indolicidin is a cationic 13 amino acid peptide amide produced in the granules of bovine neutrophils with the sequence H‐ILPWKWPWWPWRR‐NH2. Indolicidin is both antimicrobial and, to a lesser extent, haemolytic. In order to systematically investigate structure–function relationships, the solid‐phase synthesis of indolicidin and 48 distinct analogues are reported, as well as the characterization of their respective biological properties. Peptides synthesized and characterized include analogues with modified terminal functions, truncations from either terminus, an alanine scan to determine the role of each individual amino acid, specific amino acid exchanges of aromatic, charged and structural residues and several retro‐, inverso‐ and retroinverso‐analogues. Together, characterization of these analogues identifies specific residues involved in antimicrobial or haemolytic activity and suggests a core structure that may form a scaffold for the further development of peptidomimetic analogues of indolicidin. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.
ISSN:1075-2617
1099-1387
DOI:10.1002/psc.351