Synthetic mimics of antimicrobial peptides--a versatile ring-opening metathesis polymerization based platform for the synthesis of selective antibacterial and cell-penetrating polymers.
Natural macromolecules exhibit an extensive arsenal of properties, many of which have proven difficult to recapitulate in simpler synthetic systems. Over the last couple of years, foldamers have emerged as one important step toward increased functionality in synthetic systems. While the great majority of work in this area has focused on folded structures, hence the name, more recent progress has centered on polymers that mimic protein function. These efforts have resulted in the design of relatively simple macromolecules; one example are the synthetic mimics of antimicrobial peptides (SMAMPs) that capture the central physicochemical features of their natural archetypes irrespective of the specific folded form. Here we present our recent efforts to create polymers which display biological activity similar to natural proteins, including antimicrobial and cell-penetrating peptides.
Department of Polymer Science & Engineering, University of Massachusetts, Amherst, MA 01003, USA.
Karen
K
Lienkamp
Gregory N
GN
Tew
D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D040761:Biomimetic Materials / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D002477:Cells / Q000378:metabolism*; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D011108:Polymers / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D023181:Antimicrobial Cationic Peptides; D011108:Polymers