Structure–function relationships in the tryptophan‐rich, antimicrobial peptide indolicidin

Citations Over TimeTop 10% of 2001 papers

Abstract

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.

Related Papers

• → Solid‐Phase Synthesis of Peptidomimetics with Peptide Backbone Modifications(2021)20 cited
• → A hierarchical approach to peptidomimetic design(1993)152 cited
• → Peptide and peptidomimetic libraries(1998)25 cited
• → One-Pot High-Throughput Synthesis of β-Turn Cyclic Peptidomimetics via “Volatilizable” Supports(2009)7 cited
• → Synthesis and Properties of New Fluorinated Peptidomimetics(2005)3 cited