Separate Molecular Determinants in Amyloidogenic and Antimicrobial Peptides |
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| Authors: | Michael Landreh Jan Johansson Hans Jörnvall |
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| Institution: | 1 Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden;2 KI Alzheimer''s Disease Research Center, Department of Neurobiology, Care Sciences and Society, Karolinska Institutet, S-141 86 Stockholm, Sweden;3 Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, S-751 23 Uppsala, Sweden |
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| Abstract: | Several amyloid-forming and antimicrobial peptides (AMYs and AMPs) have the ability to bind to and damage cell membranes. In addition, some AMYs possess antimicrobial activity and some AMPs form amyloid-like fibrils, relating the two peptide types and their properties. However, a comparison of their sequence characteristics reveals important differences. The high β-strand and aggregation propensities typical of AMYs are largely absent in α-helix-forming AMPs, which are instead marked by a strong amphipathic moment not generally found in AMYs. Although a few peptides, for example, islet amyloid polypeptide and dermaseptin S9, combine some determinants of both groups, the structural distinctions suggest that antimicrobial activity and amyloid formation are separate features not generally associated. |
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| Keywords: | AMP antimicrobial peptide AMY amyloidogenic peptide SAA serum amyloid A hIAPP human islet amyloid polypeptide Aβ42 amyloid β 1&ndash 42 peptide MD molecular dynamics |
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