Arginine/Tryptophan‐Rich Cyclic α/β‐Antimicrobial Peptides: The Roles of Hydrogen Bonding and Hydrophobic/Hydrophilic Solvent‐Accessible Surface Areas upon Activity and Membrane Selectivity-Reference-Cited by-同舟云学术

Arginine/Tryptophan‐Rich Cyclic α/β‐Antimicrobial Peptides: The Roles of Hydrogen Bonding and Hydrophobic/Hydrophilic Solvent‐Accessible Surface Areas upon Activity and Membrane Selectivity

Published:2018-08-22 Issue:53 Volume:24 Page:14242-14253
ISSN:0947-6539
Container-title:Chemistry – A European Journal
language:en
Short-container-title:Chem. Eur. J.

Author:

Bagheri Mojtaba¹^ORCID,Amininasab Mehriar²,Dathe Margitta³

Affiliation:

1. Peptide Chemistry LaboratoryInstitute of Biochemistry and BiophysicsUniversity of Tehran 16 Azar Street 14176-14335 Tehran Iran

2. Department of cell and molecular BiologySchool of BiologyCollege of ScienceUniversity of Tehran Iran

3. Leibniz institute of molecular pharmacology (FMP) Robert Roessle Street 10 13125 Berlin Germany

Funder

Iran National Science Foundation

Publisher

Wiley

Subject

General Chemistry,Catalysis,Organic Chemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/chem.201802881

Reference76 articles.

1. Antibacterial drug discovery in the resistance era

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3. Combination Effects of Antimicrobial Peptides

4. Tryptic Stability of Synthetic Bactenecin Derivatives Is Determined by the Side Chain Length of Cationic Residues and the Peptide Conformation

5. M. Bagheri R. E. W. Hancock Methods Mol. Biol. Vol. 1548 2017 Humana Press New York 61 71

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