| Literature DB >> 27010220 |
Amanda J H Gilliam1, Joshua N Smith1, Dylan Flather1, Kevin M Johnston1, Andrew M Gansmiller1, Dmitry A Fishman1, Joshua M Edgar1, Mark Balk1, Sudipta Majumdar1, Gregory A Weiss1.
Abstract
Caveolin-1 is a target for academic and pharmaceutical research due to its many cellular roles and associated diseases. We report peptide WL47 (1), a small, high-affinity, selective disrupter of caveolin-1 oligomers. Developed and optimized through screening and analysis of synthetic peptide libraries, ligand 1 has 7500-fold improved affinity compared to its T20 parent ligand and an 80% decrease in sequence length. Ligand 1 will permit targeted study of caveolin-1 function.Entities:
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Year: 2016 PMID: 27010220 PMCID: PMC5529100 DOI: 10.1021/acs.jmedchem.5b01536
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 7.446