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Harnessing the evolvability of tricyclic microviridins to dissect protease-inhibitor interactions

  • Understanding and controlling proteolysis is an important goal in therapeutic chemistry. Among the natural products specifically inhibiting proteases microviridins are particularly noteworthy. Microviridins are ribosomally produced and posttranslationally modified peptides that are processed into a unique, cagelike architecture. Here, we report a combined rational and random mutagenesis approach that provides fundamental insights into selectivity-conferring moieties of microviridins. The potent variant microviridin J was co-crystallized with trypsin, and for the first time the three-dimensional structure of microviridins was determined and the mode of inhibition revealed.

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Metadaten
Author:Annika R. Weiz, Keishi Ishida, Felix Quitterer, Sabine Meyer, Jan-Christoph KehrGND, Kristian M. Mueller, Michael Groll, Christian Hertweck, Elke Dittmann-ThünemannORCiDGND
DOI:https://doi.org/10.1002/anie.201309721
ISSN:1433-7851
ISSN:1521-3773
Pubmed Id:http://www.ncbi.nlm.nih.gov/pubmed?term=24591244
Parent Title (English):Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition
Publisher:Wiley-VCH
Place of publication:Weinheim
Document Type:Article
Language:English
Year of first Publication:2014
Year of Completion:2014
Release Date:2017/03/27
Tag:RiPPs; cyanobacteria; peptide engineering; protease inhibitors; structure elucidation
Volume:53
Issue:14
Pagenumber:4
First Page:3735
Last Page:3738
Funder:German Research foundation (DFG) [Di910/4-1, He3469/4-1]; grant in the cluster of excellence UniCAT
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer Review:Referiert