Antimicrobial peptides: A natural alternative to chemical antibiotics and a potential for applied biotechnology

Marshall, Sergio H.; Arenas, Gloria

doi:10.2225/vol6-issue3-fulltext-1

Cited by 144 publications

(131 citation statements)

References 58 publications

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“…In the recent years, AMP-s have drawn much attention as a potentially effective class of anti-infectious therapeutics. Considering the facts that bacterial resistance to antimicrobial peptides is infrequent [12,13,8], they are non-toxic and non-immunogenic (according to numerous reports, such as [14]), extensive research programs have been established with the aim to exploit the AMP-s as a novel stand-alone class of antibiotics.…”

Section: Cationic Polypeptides As a Novel Class Of Antibacterial Thermentioning

confidence: 99%

Application of ‘Inductive’ QSAR Descriptors for Quantification of Antibacterial Activity of Cationic Polypeptides

Cherkasov

Jankovic²

2004

Molecules

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Abstract:On the basis of the inductive QSAR descriptors we have created a neural network-based solution enabling quantification of antibacterial activity in the series of 101 synthetic cationic polypeptides (CAMEL-s). The developed QSAR model allowed 80% correct categorical classification of antibacterial potencies of the CAMEL-s both in the training and the validation sets. The accuracy of the activity predictions demonstrates that a narrow set of 3D sensitive 'inductive' descriptors can adequately describe the aspects of intra-and intermolecular interactions that are relevant for antibacterial activity of the cationic polypeptides. The developed approach can be further expanded for the larger sets of biologically active peptides and can serve as a useful quantitative tool for rational antibiotic design and discovery.

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Section: Cationic Polypeptides As a Novel Class Of Antibacterial Thermentioning

confidence: 99%

Application of ‘Inductive’ QSAR Descriptors for Quantification of Antibacterial Activity of Cationic Polypeptides

Cherkasov

Jankovic²

2004

Molecules

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“…Therefore, new antimicrobial strategies and/or alternative drugs are required to revive the potency of traditional antibiotics and to guard human health (Marshall and Arenas, 2003;Marr et al, 2006). Antimicrobial peptides (AMPs) represent such a new class of antibiotics.…”

Section: Introductionmentioning

confidence: 99%

“…(4) Physiological significance; AMPs not only exhibit the ability to kill or inhibit pathogenic microorganisms, but also play an important role in modulating the immune system in vivo. (5) Wide spectrum of killing activity; AMPs have been reported to kill or inhibit a variety of organisms or cells, including Gram-negative and Gram-positive bacteria, viruses, protozoa, parasites, fungi and even cancer cells (Marshall and Arenas, 2003;Jenssen et al, 2006). Although AMPs are highly variable, most experts agree that AMPs are short peptides with 12-100 amino acids (Hancock, 1997;Jenssen et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

2010

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Antimicrobial peptides (AMPs), with their extraordinary properties, such as broad-spectrum activity, rapid action and difficult development of resistance, have become promising molecules as new antibiotics. Despite their various mechanisms of action, the interaction of AMPs with the bacterial cell membrane is the key step for their mode of action. Moreover, it is generally accepted that the membrane is the primary target of most AMPs, and the interaction between AMPs and eukaryotic cell membranes (causing toxicity to host cells) limits their clinical application. Therefore, researchers are engaged in reforming or de novo designing AMPs as a 'singleedged sword' that contains high antimicrobial activity yet low cytotoxicity against eukaryotic cells. To improve the antimicrobial activity of AMPs, the relationship between the structure and function of AMPs has been rigorously pursued. In this review, we focus on the current knowledge of α-helical cationic antimicrobial peptides, one of the most common types of AMPs in nature.

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“…The search for and development of new antibiotic compounds was identified as a task of global importance in the recent O'Neil report to the United Kingdom government on the reduction of the widespread increase in microorganism resistance (O'Neill 2015). Several recently investigated cationic peptides are currently undergoing clinical trials (Marshall and Arenas 2003;Arias and Murray 2009;Yeung et al 2011;Bahar and Ren 2013).…”

Section: Introductionmentioning

confidence: 99%

Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides

2017

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The indiscriminate use of conventional antibiotics is leading to an increase in the number of resistant bacterial strains, motivating the search for new compounds to overcome this challenging problem. Antimicrobial peptides, acting only in the lipid phase of membranes without requiring specific membrane receptors as do conventional antibiotics, have shown great potential as possible substituents of these drugs. These peptides are in general rich in basic and hydrophobic residues forming an amphipathic structure when in contact with membranes. The outer leaflet of the prokaryotic cell membrane is rich in anionic lipids, while the surface of the eukaryotic cell is zwitterionic. Due to their positive net charge, many of these peptides are selective to the prokaryotic membrane. Notwithstanding this preference for anionic membranes, some of them can also act on neutral ones, hampering their therapeutic use. In addition to the electrostatic interaction driving peptide adsorption by the membrane, the ability of the peptide to perturb lipid packing is of paramount importance in their capacity to induce cell lysis, which is strongly dependent on electrostatic and hydrophobic interactions. In the present research, we revised the adsorption of antimicrobial peptides by model membranes as well as the perturbation that they induce in lipid packing. In particular, we focused on some peptides that have simultaneously acidic and basic residues. The net charges of these peptides are modulated by pH changes and the lipid composition of model membranes. We discuss the experimental approaches used to explore these aspects of lipid membranes using lipid vesicles and lipid monolayer as model membranes.

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Antimicrobial peptides: A natural alternative to chemical antibiotics and a potential for applied biotechnology

Cited by 144 publications

References 58 publications

Application of ‘Inductive’ QSAR Descriptors for Quantification of Antibacterial Activity of Cationic Polypeptides

Application of ‘Inductive’ QSAR Descriptors for Quantification of Antibacterial Activity of Cationic Polypeptides

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides

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