Ontology highlight
ABSTRACT:
SUBMITTER: Hahn ME
PROVIDER: S-EPMC3608426 | biostudies-literature | 2013 Apr
REPOSITORIES: biostudies-literature
Hahn Michael E ME Randolph Lyndsay M LM Adamiak Lisa L Thompson Matthew P MP Gianneschi Nathan C NC
Chemical communications (Cambridge, England) 20130401 28
Polymers of norbornenyl-modified peptide-based enzyme substrates have been prepared via ring-opening metathesis polymerization (ROMP). Peptides displayed on water-soluble homopolymers retain the ability to be enzymatically processed by a disease-associated enzyme. In contrast, when the peptides are densely arrayed on a nanoparticle derived from a self-assembled amphiphilic block-copolymer, they function with reduced activity as enzymatic substrates. ...[more]