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Three‐in‐One Chromatography‐Free Purification, Tag Removal, and Site‐Specific Modification of Recombinant Fusion Proteins Using Sortase A and Elastin‐like Polypeptides
Author(s) -
Bellucci Joseph J.,
Amiram Miriam,
Bhattacharyya Jayanta,
McCafferty Dewey,
Chilkoti Ashutosh
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201208292
Subject(s) - sortase a , recombinant dna , chemistry , sortase , elastin , biochemistry , computational biology , computer science , combinatorial chemistry , biology , gene , bacterial protein , genetics
Sorting it out : Applied in tandem, elastin‐like polypeptides (ELPs, see scheme) and the Sortase A (SrtA) transpeptidase provide a method for chromatography‐free purification of recombinant proteins and optional, site‐specific conjugation of the protein to a small molecule (yellow). This system provides an efficient mechanism for generating bioactive proteins at high yields and purities.