Document Detail


Polymerization of a peptide-based enzyme substrate.
MedLine Citation:
PMID:  23450132     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Michael E Hahn; Lyndsay M Randolph; Lisa Adamiak; Matthew P Thompson; Nathan C Gianneschi
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Chemical communications (Cambridge, England)     Volume:  49     ISSN:  1364-548X     ISO Abbreviation:  Chem. Commun. (Camb.)     Publication Date:  2013 Apr 
Date Detail:
Created Date:  2013-03-13     Completed Date:  2013-09-10     Revised Date:  2014-05-07    
Medline Journal Info:
Nlm Unique ID:  9610838     Medline TA:  Chem Commun (Camb)     Country:  England    
Other Details:
Languages:  eng     Pagination:  2873-5     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Enzymes / metabolism*
Humans
Nanoparticles / chemistry
Oligopeptides / chemistry*,  metabolism*
Polymerization*
Proteolysis
Grant Support
ID/Acronym/Agency:
1DP2OD008724/OD/NIH HHS; 1R01EB011633/EB/NIBIB NIH HHS; 5T32EB005970/EB/NIBIB NIH HHS; R01 EB011633/EB/NIBIB NIH HHS; R01 HL117326/HL/NHLBI NIH HHS; R01HL117326/HL/NHLBI NIH HHS; T32 EB005970/EB/NIBIB NIH HHS
Chemical
Reg. No./Substance:
0/Enzymes; 0/Oligopeptides
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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