Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 59, Issue 24, Pages 9398-9402Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202002639
Keywords
cancer; peptide; peptidomimetics; protein-protein interactions; uPAR
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Funding
- DoD BCRP Breakthrough Award [BC141561]
- CPRIT [RP170144, RP180875]
- Robert A. Welch Foundation [A-1121]
- Texas AM University [RP180875]
- NIH/NIBIB [R01Ey02965]
- NSF [CHE1608009]
- National Science Foundation [DBI-9970232]
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Secondary structures tend to be recognizable because they have repeating structural motifs, but mimicry of these does not have to follow such well-defined patterns. Bioinformatics studies to match side-chain orientations of a novel hydantoin triazole chemotype (1) to protein-protein interfaces revealed it tends to align well across parallel and antiparallel sheets, like rungs on a ladder. One set of these overlays was observed for the protein-protein interaction uPA.uPAR. Consequently, chemotype 1 was made with appropriate side-chains to mimic uPA at this interface. Biophysical assays indicate these compounds did in fact bind uPAR, and elicit cellular responses that affected invasion, migration, and wound healing.
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