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In Vitro Discriminative Antipseudomonal Properties Resulting from Acyl Substitution of N-Terminal Sequence of Dermaseptin S4 Derivatives by Keren Marynka; Shahar Rotem; Irina Portnaya; Uri Cogan; Amram Mor is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Truncation and acylation were combined to investigate the broad-spectrum bactericidal and hemolytic peptide S4(1-15). Substitution of up to seven residues with dodecanoic acid (C 12 ) gradually led to specific antipseudomonal activity: out of 40 bacterial strains tested in vitro, C 12 -S4(8-15) displayed similar minimal inhibitory concentrations (MICs) as S4(1-15) against Pseudomonas aeruginosa sp. (identical MIC 90 ) but was practically inactive against most other bacteria or erythrocytes. Surface plasmon resonance and isothermal titration calorimetry experiments revealed the binding properties of S4(1-15) to be consistent with its nonselective activities, while discriminative activities of C 12 -S4(8-15) correlated with high binding affinity to a membrane containing pseudomonal lipopolysaccharides and with lower affinities to membranes containing nonpseudomonal lipopolysaccharides or cholesterol. Various mechanistic studies failed to detect significant differences in secondary structure, bactericidal kinetics, or ability to perturb the cytoplasmic membrane, pointing to a similar mode of action.

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Author

Keren Marynka; Shahar Rotem; Irina Portnaya; Uri Cogan; Amram Mor

Publisher

Elsevier Science; Elsevier ; Cell Press; Elsevier BV (ISSN 1074-5521)

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)