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Molecules 2014, 19(8), 10803-10817; doi:10.3390/molecules190810803

Effects of Single Amino Acid Substitution on the Biophysical Properties and Biological Activities of an Amphipathic α-Helical Antibacterial Peptide Against Gram-Negative Bacteria

1,3,†, 4,†, 1,2,3 and 1,2,3,*
1
Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun 130012, China
2
National Engineering Laboratory for AIDS Vaccine, Jilin University, Changchun 130012, China
3
School of Life Sciences, Jilin University, Changchun 130012, China
4
School of Life Sciences, Northeast Normal University, Changchun 130012, China
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Received: 6 June 2014 / Revised: 6 July 2014 / Accepted: 16 July 2014 / Published: 24 July 2014
(This article belongs to the Special Issue Peptide Chemistry)
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Abstract

An antimicrobial peptide, known as V13K, was utilized as the framework to study the effects of charge, hydrophobicity and helicity on the biophysical properties and biological activities of α-helical peptides. Six amino acids (Lys, Glu, Gly, Ser, Ala, and Leu) were individually used to substitute the original hydrophobic valine at the selected sixteenth location on the non-polar face of V13K. The results showed that the single amino acid substitutions changed the hydrophobicity of peptide analogs as monitored by RP-HPLC, but did not cause significant changes on peptide secondary structures both in a benign buffer and in a hydrophobic environment. The biological activities of the analogs exhibited a hydrophobicity-dependent behavior. The mechanism of peptide interaction with the outer membrane and cytoplasmic membrane of Gram-negative bacteria was investigated. We demonstrated that this single amino acid substitution method has valuable potential for the rational design of antimicrobial peptides with enhanced activities. View Full-Text
Keywords: antimicrobial peptide; hydrophobicity; biological activity; Gram-negative bacteria; mechanism of action antimicrobial peptide; hydrophobicity; biological activity; Gram-negative bacteria; mechanism of action
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Tan, J.; Huang, J.; Huang, Y.; Chen, Y. Effects of Single Amino Acid Substitution on the Biophysical Properties and Biological Activities of an Amphipathic α-Helical Antibacterial Peptide Against Gram-Negative Bacteria. Molecules 2014, 19, 10803-10817.

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