Structure, Interactions, and Antibacterial Activities of MSI-594 Derived Mutant Peptide MSI-594F5A in Lipopolysaccharide Micelles: Role of the Helical Hairpin Conformation in Outer-Membrane Permeabilization-Reference-Cited by-同舟云学术

Structure, Interactions, and Antibacterial Activities of MSI-594 Derived Mutant Peptide MSI-594F5A in Lipopolysaccharide Micelles: Role of the Helical Hairpin Conformation in Outer-Membrane Permeabilization

Published:2010-12-03 Issue:51 Volume:132 Page:18417-18428
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Domadia Prerna N¹,Bhunia Anirban¹,Ramamoorthy Ayyalusamy¹,Bhattacharjya Surajit¹

Affiliation:

1. School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore-637551 and Department of Chemistry and Biophysics, University of Michigan, Ann Arbor, Michigan 48109-1055, United States United States of America

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja1083255

Reference84 articles.

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2. Antibacterial resistance worldwide: causes, challenges and responses

3. Microbiology and drug resistance mechanisms of fully resistant pathogens

4. Controlling Antimicrobial Resistance in Hospitals: Infection Control and Use of Antibiotics

5. The Bacteria Fight Back

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