Protein & Peptide Letters

Author(s): David Wade, Jan-Ingmar Flock, Charlotta Edlund, Ingegerd Lofving-Arvholm, Matti Sallberg, Tomas Bergman, Angela Silveira, Cecille Unson, Louise Rollins-Smith, Jerzy Silberring, Malcom Richardson, Pentti Kuusela and Hilkka Lankinen

DOI: 10.2174/0929866023408409

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Antibiotic Properties of Novel Synthetic Temporin A Analogs and a Cecropin A-Temporin A Hybrid Peptide

Page: [533 - 543] Pages: 11

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Abstract

Temporin A, 18 analogs, and a cecropin A-temporin A hybrid peptide were tested with antibiotic sensitive and resistant bacteria, fungi, human erythrocytes, and in clotting assays.Several peptides were active in these assays, and some analogs (D-TA, W1-TA, and Con-L4,G10) may be useful lead compounds for further antibiotics development.The activity of temporin A was found to be dependent upon several of its structural features, including amino acid composition and sequence, chirality, helicity, and positive charge.

Keywords: temporin a, cecropin a, vescp-m, ranatuerin 6, antibiotic peptides, antibiotic resistant bacteria, antifungal, human erythrocyte lysis, hemolysis