Role of Lipopolysaccharide in protecting OmpT from autoproteolysis during in vitro refolding
Outer membrane protease (OmpT) is a 33.5 kDa aspartyl protease that cleaves at dibasic sites and is thought to function as a defense mechanism for E. coli against cationic antimicrobial peptides secreted by the host immune system. Despite carrying three dibasic sites in its own sequence, there is no...
Saved in:
Main Authors: | Sinsinbar, Gaurav, Gudlur, Sushanth, Metcalf, Kevin J., Mrksich, Milan, Nallani, Madhavan, Liedberg, Bo |
---|---|
Other Authors: | School of Materials Science and Engineering |
Format: | Article |
Language: | English |
Published: |
2020
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/144253 https://doi.org/10.3390/biom10060922 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | Nanyang Technological University |
Language: | English |
Similar Items
-
Outer-Membrane Protease (OmpT) based E. coli sensing with anionic polythiophene and unlabeled peptide substrate
by: Sinsinbar, Gaurav, et al.
Published: (2020) -
Recombinant factor C competes against LBP to bind lipopolysaccharide and neutralizes the endotoxicity
by: Li, P., et al.
Published: (2011) -
Inhibition of OmpT activity using D-amino acid peptides
by: Lim, Ernest Jun Wei
Published: (2020) -
Role of Aromatic Amino Acids in Lipopolysaccharide and Membrane Interactions of Antimicrobial Peptides for Use in Plant Disease Control
by: Datta, Aritreyee, et al.
Published: (2016) -
NMR Structures and Interactions of Antimicrobial Peptides with Lipopolysaccharide: Connecting Structures to Functions
by: Bhattacharjya, Surajit
Published: (2016)