Cooperative Modes of Action of Antimicrobial Peptides Characterized with Atomistic Simulations: A Study on Cecropin B
Author:
Affiliation:
1. Scientific Computing Department, STFC Daresbury Laboratory, Keckwick Lane, Daresbury, Warrington WA4 4AD, U.K.
2. Clay Technology AB, Ideon Science Park, SE-223 70 Lund, Sweden
3. IBM Research, Hartree Centre, Daresbury WA4 4AD, U.K.
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.8b01957
Reference57 articles.
1. Rivas, L.; Andreu, D. Pore Forming Peptides and Protein Toxins; Menestrina, G., Menestrina, G., Serra, M. D., Lazarovici, P., Eds. CRC Press, 2003; pp 209–259.
2. Mode of action of membrane active antimicrobial peptides
3. Initial Binding Sites of Antimicrobial Peptides in Staphylococcus aureus and Escherichia coli
4. Bacterial membrane lipids: diversity in structures and pathways
5. Bacterial strategies of resistance to antimicrobial peptides
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3. Expression of Antimicrobial Peptide (AMP), Cecropin B, in a Fused Form to SUMO Tag With or Without Three-Glycine Linker in Escherichia coli and Evaluation of Bacteriolytic Activity of the Purified AMP;Probiotics and Antimicrobial Proteins;2021-05-20
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