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Synthesis of a 2-arylsulphonylated tryptophan: the antibacterial activity of bovine lactoferricin peptides containing Trp(2-Pmc)

✍ Scribed by Bengt Erik Haug; Jill Andersen; Øystein Rekdal; Dr John S. Svendsen

Book ID: 105360215
Publisher: John Wiley and Sons
Year: 2002
Tongue: English
Weight: 99 KB
Volume: 8
Category: Article
ISSN: 1075-2617
DOI: 10.1002/psc.404

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✦ Synopsis

Abstract

A modified tryptophan, β‐[2‐(2,2,5,7,8‐pentamethylchroman‐6‐sulphonyl)‐indol‐3‐yl]alanine, Trp(2 − Pmc) = Tpc has been synthesized. Replacement of tryptophan in a bovine lactoferricin model peptide with the modified tryptophan resulted in peptides with a substantially increased antibacterial activity against Escherichia coli and Staphylococcus aureus. The most active peptides against each bacterial strain displayed minimal inhibitory concentrations of 7.5 μg/ml. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.

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✍ Bengt Erik Haug; John S Svendsen 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 81 KB

## Abstract Bovine lactoferricin is a 25‐residue antibacterial peptide isolated after gastric cleavage of the iron transporting protein lactoferrin. A 15‐residue fragment, FKCRRWQWRMKKLGA of this peptide sustains most of the antibacterial activity. In this truncated sequence, the two Trp residues a