Structural determinants of antimicrobial activity in polymers which mimic host defense peptides

被引:0
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作者
Edmund F. Palermo
Kenichi Kuroda
机构
[1] University of Michigan,Macromolecular Science and Engineering Center
[2] University of Michigan,Department of Biologic and Materials Sciences, School of Dentistry
来源
关键词
Antimicrobial; Polymer; Peptide mimic; Structure−activity; Membrane disruption; Cell penetrating;
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摘要
Antimicrobial polymers, designed to mimic the salient structural features of host defense peptides, are an emerging class of materials with potential for applications to combat infectious disease. Because the putative mode of action relies on physiochemical parameters of peptides such as hydrophobicity and cationic charge, rather than specific receptor-mediated interactions, the activity of the polymers can be modulated by tuning key structural parameters. While a wide diversity of chemical structures have been reported as antimicrobial polymers, a precise understanding of the structural factors which control their activity is a subject of current investigations. In this mini-review, we will outline the design principles that have been developed so far to fine tune the activity of these antimicrobial agents. The roles played by specific structural features such as cationic charge, hydrophobicity, and molecular weight will be discussed. Future directions of the field and potential challenges will be proposed.
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页码:1605 / 1615
页数:10
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