Cyclic peptide production using a macrocyclase with enhanced substrate promiscuity and relaxed recognition determinants

Autor:	Wael E. Houssen, David P. Fewer, Cristina N. Alexandru-Crivac, Christian Umeobika, Kaarina Sivonen, Jouni Jokela, Laurent Trembleau, Niina Leikoski, Eike Siebs, Matti Wahlsten, Mohannad Idress, Peter Sjö, André M. Grilo, Ada F. Nneoyiegbe, Marcel Jaspars, Alleyn T. Plowright, Kirstie A. Rickaby
Rok vydání:	2017
Předmět:	0301 basic medicine Macrocyclic Compounds Stereochemistry Peptide Molecular Dynamics Simulation Peptides Cyclic 01 natural sciences Chemical synthesis Gene Expression Regulation Enzymologic Catalysis Substrate Specificity 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Biosynthesis Materials Chemistry chemistry.chemical_classification 010405 organic chemistry Drug discovery Thiazoline Metals and Alloys Substrate (chemistry) Gene Expression Regulation Bacterial General Chemistry Peptide Fragments Cyclic peptide 0104 chemical sciences Surfaces Coatings and Films Electronic Optical and Magnetic Materials Amino acid 030104 developmental biology chemistry Cyclization Oscillatoria Ceramics and Composites
Zdroj:	Chemical Communications. 53:10656-10659
ISSN:	1364-548X 1359-7345
DOI:	10.1039/c7cc05913b
Popis:	Macrocyclic peptides have promising therapeutic potential but the scaling up of their chemical synthesis is challenging. The cyanobactin macrocyclase PatGmac is an efficient tool for production but is limited to substrates containing 6–11 amino acids and at least one thiazoline or proline. Here we report a new cyanobactin macrocyclase that can cyclize longer peptide substrates and those not containing proline/thiazoline and thus allows exploring a wider chemical diversity.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4de2b24c76f3b31412117255bc7d984 https://doi.org/10.1039/c7cc05913b Zobrazit plný text záznamu