Biochemical and structural characterization of intein inhibitors for use as anti-mycobacterial therapeutics

Authors
Chan, Hon
ORCID
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Other Contributors
Belfort, Georges
Belfort, Marlene
Karande, Pankaj
Koffas, Mattheos A. G.
Issue Date
2015-12
Keywords
Chemical engineering
Degree
MS
Terms of Use
This electronic version is a licensed copy owned by Rensselaer Polytechnic Institute, Troy, NY. Copyright of original work retained by author.
Full Citation
Abstract
The human pathogen Mycobacterium tuberculosis harbor inteins, self-splicing protein elements, in critical dnaB, recA and sufB genes. Inteins render the host protein non-functional until splicing occurs, thus inhibition of splicing provides a novel target for design of anti-mycobacterial compounds. The splicing inhibition of a minimized RecA intein (Mini-RecAi) was investigated, firstly through a screening a series of candidate molecules. Secondly the binding of cisplatin, a FDA approved chemotherapeutic and potent inhibitor of Mini-RecAi, was characterized using mass spectrometry, nuclear magnetic resonance and crystallographic methods.
Description
December 2015
School of Engineering
Department
Dept. of Chemical and Biological Engineering
Publisher
Rensselaer Polytechnic Institute, Troy, NY
Relationships
Rensselaer Theses and Dissertations Online Collection
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