Interfacial Self-Assembly of Antimicrobial Peptide GL13K into Non-Fibril Crystalline β-Sheets-Reference-Cited by-同舟云学术

Interfacial Self-Assembly of Antimicrobial Peptide GL13K into Non-Fibril Crystalline β-Sheets

Published:2019-12-27 Issue:2 Volume:36 Page:660-665
ISSN:0743-7463
Container-title:Langmuir
language:en
Short-container-title:Langmuir

Author:

Youssef Hala¹,DeWolf Christine E.¹^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry and Centre for NanoScience Research, Concordia University, 7141 Sherbrooke Street West, Montreal H4B 1R6, Canada

Funder

Canada Foundation for Innovation

Natural Sciences and Engineering Research Council of Canada

National Science Foundation

Argonne National Laboratory

Publisher

American Chemical Society (ACS)

Subject

Electrochemistry,Spectroscopy,Surfaces and Interfaces,Condensed Matter Physics,General Materials Science

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.langmuir.9b03120

Reference55 articles.

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3. Antimicrobial peptide, tachyplesin I, isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus). NMR determination of the beta-sheet structure.

4. The antimicrobial peptide gramicidin S permeabilizes phospholipid bilayer membranes without forming discrete ion channels

5. Three-Dimensional Structure of RTD-1, a Cyclic Antimicrobial Defensin from Rhesus Macaque Leukocytes,

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