Directed sortase A evolution for efficient site-specific bioconjugations in organic co-solvents

Autor:	Ulrich Schwaneberg, Hoda Alibiglou, Felix Jakob, Zhi Zou, Diana M. Mate, Mehdi D. Davari
Rok vydání:	2018
Předmět:	Staphylococcus aureus Stereochemistry Molecular Dynamics Simulation Protein Engineering 010402 general chemistry 01 natural sciences Catalysis Molecular dynamics Bacterial Proteins Materials Chemistry Dimethyl Sulfoxide Amino Acid Sequence Peptide sequence Co solvent Ethanol 010405 organic chemistry Chemistry Methanol Mutagenesis Metals and Alloys Water Dimethylformamide General Chemistry Protein engineering Aminoacyltransferases 0104 chemical sciences Surfaces Coatings and Films Electronic Optical and Magnetic Materials Cysteine Endopeptidases Sortase A Mutation Mutagenesis Site-Directed Solvents Ceramics and Composites Directed Molecular Evolution Peptides
Zdroj:	Chemical Communications. 54:11467-11470
ISSN:	1364-548X 1359-7345
DOI:	10.1039/c8cc06017g
Popis:	Directed sortase A evolution yielded the variants R159G and D165Q/D186G/K196V with increased resistance (2.2-fold) and catalytic efficiency (6.3-fold) in 45% (v/v) dimethylsulfoxide. Interestingly, D165Q/D186G/K196V also showed an up to 4.7-fold increased activity for the conjugation of hydrophobic peptides/amines in co-solvents. MD simulations revealed that conformational mobilities are important for the gained resistance.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::365299c0aff65aa06f1929735ecfe87d https://doi.org/10.1039/c8cc06017g Zobrazit plný text záznamu