期刊
JOURNAL OF CHROMATOGRAPHY A
卷 1053, 期 1-2, 页码 161-172出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.chroma.2004.08.137
关键词
hydrophilicity; hydrophobicity; amphipathicity; antimicrobial peptides
资金
- NIGMS NIH HHS [R01 GM061855-05, R01GM61855] Funding Source: Medline
The ability to monitor precisely the hydrophobicity/hydrophilicity effects of amino acid substitutions in both the non-polar and polar faces of amphipathic alpha-helical peptides is critical in such areas as the rational de novo design of more effective antimicrobial peptides. The present study reports our initial results of employing the complementary separation modes of reversed-phase high-performance liquid chromatography (RP-HPLC) and hydrophilic interaction/cation-exchange chromatography (HILIC/CEX) to monitor the effect on apparent peptide hydrophilicity/hydrophobicity and amphipathicity of substituting single L- or D-amino acids into the centre of the non-polar or polar faces of a 26-residue biologically active amphipathic a-helical peptide, V-681. Our results clearly show that RP-HPLC and HILIC/CEX are best suited for resolving amphipathic peptides where substitutions are made in the non-polar and polar faces, respectively. Further, RP-HPLC and HILIC/CEX were demonstrated to be excellent monitors of hydrophilicity/hydrophobicity variations where amino acid substitutions were made in these respective faces. We believe these complementary high-performance modes offer excellent potential for rational design of novel amphipathic alpha-helical biologically active peptides. (C) 2004 Elsevier B.V. All rights reserved.
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