Tryptic Stability of Synthetic Bactenecin Derivatives Is Determined by the Side Chain Length of Cationic Residues and the Peptide Conformation-Reference-Cited by-同舟云学术

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

Published:2016-03-18 Issue:7 Volume:59 Page:3079-3086
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Bagheri Mojtaba¹,Arasteh Shima¹,Haney Evan F.²,Hancock Robert E. W.²

Affiliation:

1. Peptide Chemistry Laboratory, Institute of Biochemistry and Biophysics, University of Tehran, 16 Azar Street, 14176-14335 Tehran, Iran

2. Centre for Microbial Diseases and Immunity Research, University of British Columbia, 2259 Lower Mall Research Station, Vancouver, BC V6T 1Z4, Canada

Funder

Canadian Institutes of Health Research

Iran National Science Foundation

University of Tehran

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.5b01740

Reference25 articles.

1. Designing antimicrobial peptides: form follows function

2. Strategies to prolong the plasma residence time of peptidedrugs

3. Serum Stable Natural Peptides Designed by mRNA Display

4. Metabolic Fate of Lactoferricin-Based Antimicrobial Peptides: Effect of Truncation and Incorporation of Amino Acid Analogs on the In Vitro Metabolic Stability

5. Easy Strategy To Protect Antimicrobial Peptides from Fast Degradation in Serum

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