scholarly journals Roles of Hydrophobicity and Charge Distribution of Cationic Antimicrobial Peptides in Peptide-Membrane Interactions

2012 ◽  
Vol 287 (10) ◽  
pp. 7738-7745 ◽  
Author(s):  
Lois M. Yin ◽  
Michelle A. Edwards ◽  
Jessica Li ◽  
Christopher M. Yip ◽  
Charles M. Deber
Keyword(s):  
Antimicrobial Peptides ◽  
Charge Distribution ◽  
Membrane Interactions ◽  
Cationic Antimicrobial Peptides

scholarly journals Membrane interactions of designed cationic antimicrobial peptides: The two thresholds

Biopolymers ◽  
2008 ◽  
Vol 89 (5) ◽  
pp. 360-371 ◽  
Author(s):  
Evgenia Glukhov ◽  
Lori L. Burrows ◽  
Charles M. Deber
Keyword(s):  
Antimicrobial Peptides ◽  
Membrane Interactions ◽  
Cationic Antimicrobial Peptides

Cationic Antimicrobial Peptides for Tuberculosis: A Mini-Review

2019 ◽  
Vol 20 (9) ◽  
pp. 885-892
Author(s):  
Sara Silva ◽  
Nuno Vale
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Amino Acid ◽  
Antimicrobial Peptides ◽  
Resistance Mechanisms ◽  
Therapeutic Agents ◽  
Pharmacological Properties ◽  
Therapeutic Activity ◽  
Alternative Strategies ◽  
Cationic Antimicrobial Peptides ◽  
Specific Amino Acid

Cationic antimicrobial peptides (CAMPs) can be considered as new potential therapeutic agents for Tuberculosis treatment with a specific amino acid sequence. New studies can be developed in the future to improve the pharmacological properties of CAMPs and also understand possible resistance mechanisms. This review discusses the principal properties of natural and/or synthetic CAMPs, and how these new peptides have a significant specificity for Mycobacterium tuberculosis. Also, we propose some alternative strategies to enhance the therapeutic activity of these CAMPs that include coadministration with nanoparticles and/or classic drugs.

Membrane targeting cationic antimicrobial peptides

2019 ◽  
Vol 537 ◽  
pp. 163-185 ◽  
Author(s):  
Daniela Ciumac ◽  
Haoning Gong ◽  
Xuzhi Hu ◽  
Jian Ren Lu
Keyword(s):  
Antimicrobial Peptides ◽  
Membrane Targeting ◽  
Cationic Antimicrobial Peptides

Cationic Antimicrobial Peptides in Penaeid Shrimp

2011 ◽  
Vol 13 (4) ◽  
pp. 639-657 ◽  
Author(s):  
Anchalee Tassanakajon ◽  
Piti Amparyup ◽  
Kunlaya Somboonwiwat ◽  
Premruethai Supungul
Keyword(s):  
Antimicrobial Peptides ◽  
Penaeid Shrimp ◽  
Cationic Antimicrobial Peptides

scholarly journals Generation of novel cationic antimicrobial peptides from natural non-antimicrobial sequences by acid-amide substitution

2011 ◽  
Vol 10 (1) ◽  
pp. 11 ◽  
Author(s):  
Satoshi Ueno ◽  
Masaomi Minaba ◽  
Yuji Nishiuchi ◽  
Misako Taichi ◽  
Yasushi Tamada ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Acid Amide ◽  
Cationic Antimicrobial Peptides

scholarly journals Bordetella pertussis Lipid A Glucosamine Modification Confers Resistance to Cationic Antimicrobial Peptides and Increases Resistance to Outer Membrane Perturbation

2014 ◽  
Vol 58 (8) ◽  
pp. 4931-4934 ◽  
Author(s):  
Nita R. Shah ◽  
Robert E. W. Hancock ◽  
Rachel C. Fernandez
Keyword(s):  
Immune System ◽  
Antimicrobial Peptides ◽  
Outer Membrane ◽  
Bordetella Pertussis ◽  
Lipid A ◽  
Whooping Cough ◽  
Human Immune System ◽  
Cationic Antimicrobial Peptides ◽  
Content Type ◽  
Membrane Perturbation

ABSTRACTBordetella pertussis, the causative agent of whooping cough, has many strategies for evading the human immune system. Lipopolysaccharide (LPS) is an important Gram-negative bacterial surface structure that activates the immune system via Toll-like receptor 4 and enables susceptibility to cationic antimicrobial peptides (CAMPs). We show modification of the lipid A region of LPS with glucosamine increased resistance to numerous CAMPs, including LL-37. Furthermore, we demonstrate that this glucosamine modification increased resistance to outer membrane perturbation.

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