Unconventional Secondary Structure Mimics: Ladder‐Rungs

Autor:	Kevin Burgess, Maritess Arancillo, Jonathan Whisenant, Chen-Ming Lin
Rok vydání:	2020
Předmět:	Peptidomimetic Chemistry Proteins General Medicine General Chemistry Triazoles Antiparallel (biochemistry) Urokinase-Type Plasminogen Activator Article Protein Structure Secondary Catalysis Protein–protein interaction Biomimetic Materials Biophysics Structural motif Protein secondary structure
Zdroj:	Angew Chem Int Ed Engl
ISSN:	1521-3773 1433-7851
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9803b2e9436afab42ec71c5ba2eab172 https://doi.org/10.1002/anie.202002639 Zobrazit plný text záznamu Plný text