Mode of Action of Cationic Antimicrobial Peptides Defines the Tethering Position and the Efficacy of Biocidal Surfaces

2011 ◽  
Vol 23 (1) ◽  
pp. 66-74 ◽  
Author(s):  
Mojtaba Bagheri ◽  
Michael Beyermann ◽  
Margitta Dathe
Keyword(s):  
Antimicrobial Peptides ◽  
Mode Of Action ◽  
Cationic Antimicrobial Peptides

scholarly journals Short Cationic Antimicrobial Peptides Interact with ATP

2010 ◽  
Vol 54 (10) ◽  
pp. 4480-4483 ◽  
Author(s):  
Kai Hilpert ◽  
Brett McLeod ◽  
Jessie Yu ◽  
Melissa R. Elliott ◽  
Marina Rautenbach ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Dna Polymerase ◽  
Mode Of Action ◽  
Firefly Luciferase ◽  
Cationic Antimicrobial Peptides ◽  
Dna Polymerase Α

ABSTRACT The mode of action of short, nonhelical antimicrobial peptides is still not well understood. Here we show that these peptides interact with ATP and directly inhibit the actions of certain ATP-dependent enzymes, such as firefly luciferase, DnaK, and DNA polymerase. α-Helical and planar or circular antimicrobial peptides did not show such interaction with ATP.

scholarly journals Ceragenins and antimicrobial peptides kill bacteria through distinct mechanisms

2020 ◽  
Author(s):  
Gabriel Mitchell ◽  
Melanie R. Silvis ◽  
Kelsey C. Talkington ◽  
Jonathan M. Budzik ◽  
Claire E. Dodd ◽  
...  
Keyword(s):  
Antibiotic Resistance ◽  
Antimicrobial Peptides ◽  
Mode Of Action ◽  
Essential Gene ◽  
Bacterial Species ◽  
Antimicrobial Activities ◽  
Production Costs ◽  
Cationic Antimicrobial Peptides ◽  
E Coli ◽  
Naturally Occurring

ABSTRACTCeragenins are a family of synthetic amphipathic molecules designed to mimic the properties of naturally-occurring cationic antimicrobial peptides (CAMPs). Although ceragenins have potent antimicrobial activity, whether their mode of action is similar to that of CAMPs has remained elusive. Here we report the results of a comparative study of the bacterial responses to two well-studied CAMPs, LL37 and colistin, and two ceragenins with related structures, CSA13 and CSA131. Using transcriptomic and proteomic analyses, we found that Escherichia coli responds similarly to both CAMPs and ceragenins by inducing a Cpx envelope stress response. However, whereas E. coli exposed to CAMPs increased expression of genes involved in colanic acid biosynthesis, bacteria exposed to ceragenins specifically modulated functions related to phosphate transport, indicating distinct mechanisms of action between these two classes of molecules. Although traditional genetic approaches failed to identify genes that confer high-level resistance to ceragenins, using a Clustered Regularly Interspaced Short Palindromic Repeats interference (CRISPRi) approach we identified E. coli essential genes that when knocked down modify sensitivity to these molecules. Comparison of the essential gene-antibiotic interactions for each of the CAMPs and ceragenins identified both overlapping and distinct dependencies for their antimicrobial activities. Overall, this study indicates that while some bacterial responses to ceragenins overlap with those induced by naturally-occurring CAMPs, these synthetic molecules target the bacterial envelope using a distinctive mode of action.IMPORTANCEThe development of novel antibiotics is essential since the current arsenal of antimicrobials will soon be ineffective due to the widespread occurrence of antibiotic resistance. Development of naturally-occurring cationic antimicrobial peptides (CAMPs) for therapeutics to combat antibiotic resistance has been hampered by high production costs and protease sensitivity, among other factors. The ceragenins are a family of synthetic CAMP mimics that kill a broad spectrum of bacterial species but are less expensive to produce, resistant to proteolytic degradation and have been associated with low levels of resistance. Determining how ceragenins function may identify new essential biological pathways of bacteria that are less prone to development of resistance and will further our understanding of the design principles for maximizing the effects of synthetic CAMPs.

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
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