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Role of helicity of a-helical antimicrobia peptides to improve specificity

Protein & Cell 2014年第8期5卷 631-642页

作者： Yibing Huang Liyan He Guirong Li Naicui Zhai Hongyu Jiang Yuxin Chen Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education Jilin University Changchun 130012 China National Engineering Laboratory for AIDS Vaccine Jilin University Changchun 130012 China School of Life Sciences Jilin University Changchun 130012 China The First Hospital Jilin University Changchun 130021 China

A major barrier to the use of antimicrobial peptides as antibiotics is the toxicity or ability to lyse eukaryotic cells. In this study, a 26-residue amphipathic a-helical antimicrobial peptide A12L/A20L （Ac-KWKSFLKTFKSLK KTVLHTLLKAISS-amide） was used as the framework to design a series of D- and L-diastereomeric peptides and study the relationships of helicity and biological activi- ties of o-helical antimicrobial peptides. Peptide helicity was measured by circular dichroism spectroscopy and demonstrated to correlate with the hydrophobicity of peptides and the numbers of D-amino acid substitu- tions. Therapeutic index was used to evaluate the selectivity of peptides against prokaryotic cells. By introducing D-amino acids to replace the original L-amino acids on the non-polar face or the polar face of the helix, the hemolytic activity of peptide analogs have been significantly reduced. Compared to the parent peptide, the therapeutic indices were improved of 44-fold and 22-fold against Gram-negative and Gram- positive bacteria, respectively. In addition, D- and L-diastereomeric peptides exhibited lower interaction with zwitterionic eukaryotic membrane and showed the significant membrane damaging effect to bacterial cells. Helicity was proved to play a crucial role on peptide specificity and biological activities. By simply replacing the hydrophobic or the hydrophilic amino acid residues on the non-polar or the polar face of these amphipathic derivatives of the parent peptide with D-amino acids, we demonstrated that this method could have excellent potential for the rational design of antimicrobial pep- tides with enhanced specificity.

关键词： antimicrobial peptides （AMPs） peptideantibiotics helicity secondary structure diastereomericpeptides specificity therapeutic index

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