Antimicrobial Peptides: Successes, Challenges and Unanswered Questions.
Summary of "Antimicrobial Peptides: Successes, Challenges and Unanswered Questions."
Multidrug antibiotic resistance is an increasingly serious public health problem worldwide. Thus, there is a significant and urgent need for the development of new classes of antibiotics that do not induce resistance. To develop such antimicrobial compounds, we must look toward agents with novel mechanisms of action. Membrane-permeabilizing antimicrobial peptides (AMPs) are good candidates because they act without high specificity toward a protein target, which reduces the likelihood of induced resistance. Understanding the mechanism of membrane permeabilization is crucial for the development of AMPs into useful antimicrobial agents. Various models, some phenomenological and others more quantitative or semimolecular, have been proposed to explain the action of AMPs. While these models explain many aspects of AMP action, none of the models captures all of the experimental observations, and significant questions remain unanswered. Here, we discuss the state of the field and pose some questions that, if answered, could speed the discovery of clinically useful peptide antibiotics.
Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, LA, 70112, USA, email@example.com.
This article was published in the following journal.
Name: The Journal of membrane biology
- PubMed Source: http://www.ncbi.nlm.nih.gov/pubmed/21225255
- DOI: http://dx.doi.org/10.1007/s00232-011-9343-0
Medical and Biotech [MESH] Definitions
Works consisting of compilations of questions and answers pertaining to a particular subject, used for study and review.
Antimicrobial Cationic Peptides
Small cationic peptides that are an important component, in most species, of early innate and induced defenses against invading microbes. In animals they are found on mucosal surfaces, within phagocytic granules, and on the surface of the body. They are also found in insects and plants. Among others, this group includes the DEFENSINS, protegrins, tachyplesins, and thionins. They displace DIVALENT CATIONS from phosphate groups of MEMBRANE LIPIDS leading to disruption of the membrane.
A class of antimicrobial peptides discovered in the skin of XENOPUS LAEVIS. They kill bacteria by permeabilizing cell membranes without exhibiting significant toxicity against mammalian cells.
Family of antimicrobial peptides that have been identified in humans, animals, and plants. They are thought to play a role in host defenses against infections, inflammation, wound repair, and acquired immunity.
Antimicrobial peptides of 45-47 amino acids and typically with four disulfide bridges. They are found in PLANTS. Type-V thionins lack the C-terminal nonapeptide. This should not be confused with thionine.
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