Topic
Antimicrobial peptides
About: Antimicrobial peptides is a research topic. Over the lifetime, 10645 publications have been published within this topic receiving 507688 citations. The topic is also known as: host defense peptide & antimicrobial protein.
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TL;DR: An overview of cationic antimicrobial peptides, origin, structure, functions, and mode of action of AMPs, which are highly expressed and found in humans, as well as a brief discussion about widely abundant, well characterized AMPs in mammals.
Abstract: Life-threatening infectious diseases are on their way to cause a worldwide crisis, as treating them effectively is becoming increasingly difficult due to the emergence of antibiotic resistant strains. Antimicrobial peptides (AMPs) form an ancient type of innate immunity found universally in all living organisms, providing a principal first-line of defense against the invading pathogens. The unique diverse function and architecture of AMPs has attracted considerable attention by scientists, both in terms of understanding the basic biology of the innate immune system, and as a tool in the design of molecular templates for new anti-infective drugs. AMPs are gene-encoded short (<100 amino acids), amphipathic molecules with hydrophobic and cationic amino acids arranged spatially, which exhibit broad spectrum antimicrobial activity. AMPs have been the subject of natural evolution, as have the microbes, for hundreds of millions of years. Despite this long history of co-evolution, AMPs have not lost their ability to kill or inhibit the microbes totally, nor have the microbes learnt to avoid the lethal punch of AMPs. AMPs therefore have potential to provide an important breakthrough and form the basis for a new class of antibiotics. In this review, we would like to give an overview of cationic antimicrobial peptides, origin, structure, functions, and mode of action of AMPs, which are highly expressed and found in humans, as well as a brief discussion about widely abundant, well characterized AMPs in mammals, in addition to pharmaceutical aspects and the additional functions of AMPs.
589 citations
TL;DR: Using GFP reporter transgenes, it is shown that all seven Drosophila antimicrobial peptides can be induced in surface epithelia in a tissue-specific manner and drosomycin expression, which is regulated by the Toll pathway during the systemic response, isregulated by imd in the respiratory tract, thus demonstrating the existence of distinct regulatory mechanisms for local and systemic induction of antimacterial peptide genes in Droseophila.
586 citations
TL;DR: A novel mode of action is discussed in detail, i.e., the formation of a dynamic peptide-lipid supramolecular pore, which allows the mutually coupled transbilayer transport of ions, lipids, and peptides per se.
586 citations
TL;DR: This review article summarizes the molecular basis for the cell selectivity (bacteria versus host cells) of AMPs and various attempts to control it, including the optimization of physicochemical parameters of peptide parameters, the introduction of D-, fluorinated, and unusual amino acids into peptides, the constraining of peptIDE conformations, and the modification of peptides by polymers.
583 citations
TL;DR: Strong membrane-binding and micromolar therapeutic concentrations of AMPs indicate that membrane-bound concentrations may be reached that are higher than intuitively expected, triggering disruptive effects on bacteria.
Abstract: An increasing amount of information on the action of antimicrobial peptides (AMPs) at the molecular level has not yet been translated into a comprehensive understanding of effects in bacteria. Although some biophysical attributes of AMPs have been correlated with macroscopic features, the physiological relevance of other properties has not yet been addressed. Pertinent and surprising conclusions have therefore been left unstated. Strong membrane-binding and micromolar therapeutic concentrations of AMPs indicate that membrane-bound concentrations may be reached that are higher than intuitively expected, triggering disruptive effects on bacteria.
577 citations