Journal ArticleDOI
Anti-microbial peptides: from invertebrates to vertebrates
TLDR
This review focuses on AMPs forming α‐helices, β‐hairpin‐like β‐sheets, α‐helix/β‐sheet mixed structures from invertebrate and vertebrate origins, which show some promise for therapeutic use.Abstract:
Gene-encoded anti-microbial peptides (AMPs) are widespread in nature, as they are synthesized by microorganisms as well as by multicellular organisms from both the vegetal and the animal kingdoms. These naturally occurring AMPs form a first line of host defense against pathogens and are involved in innate immunity. Depending on their tissue distribution, AMPs ensure either a systemic or a local protection of the organism against environmental pathogens. They are classified into three major groups: (i) peptides with an alpha-helical conformation (insect cecropins, magainins, etc.), (ii) cyclic and open-ended cyclic peptides with pairs of cysteine residues (defensins, protegrin, etc.), and (iii) peptides with an over-representation of some amino acids (proline rich, histidine rich, etc.). Most AMPs display hydrophobic and cationic properties, have a molecular mass below 25-30 kDa, and adopt an amphipathic structure (alpha-helix, beta-hairpin-like beta-sheet, beta-sheet, or alpha-helix/beta-sheet mixed structures) that is believed to be essential to their anti-microbial action. Interestingly, in recent years, a series of novel AMPs have been discovered as processed forms of large proteins. Despite the extreme diversity in their primary and secondary structures, all natural AMPs have the in vitro particularity to affect a large number of microorganisms (bacteria, fungi, yeast, virus, etc.) with identical or complementary activity spectra. This review focuses on AMPs forming alpha-helices, beta-hairpin-like beta-sheets, beta-sheets, or alpha-helix/beta-sheet mixed structures from invertebrate and vertebrate origins. These molecules show some promise for therapeutic use.read more
Citations
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Journal ArticleDOI
Peptide Antimicrobial Agents
TL;DR: The structural requirements of peptides for antiviral and antibacterial activities are evaluated in light of the diverse set of primary and secondary structures described for host defense peptides.
Journal ArticleDOI
Development and biological activities of marine-derived bioactive peptides: A review
Se-Kwon Kim,Isuru Wijesekara +1 more
TL;DR: An overview of the bioactive peptides derived from marine organisms and their biological activities with potential applications in different areas is presented.
Journal ArticleDOI
Melanogenesis and associated cytotoxic reactions: applications to insect innate immunity.
TL;DR: This review examines some of the factors that influence enzyme-mediated melanogenic responses, and how these responses likely contribute to blood cell-mediated, target-specific cytotoxicity in immune challenged insects.
Journal ArticleDOI
Antimicrobial peptides: general overview and clinical implications in human health and disease.
TL;DR: This review focuses on cathelicin and defensins, the most documented human AMPs, and discusses their antimicrobial activity and pleiotropic immunomodulating effects on inflammatory and infectious diseases.
Journal ArticleDOI
Phenoloxidase: a key component of the insect immune system
TL;DR: Recent progress in PO research is reviewed and some basic directions for future investigation of PO are put forward aimed at explaining its activating system, its substrates, its coordination with other immune components to fight off pathogens, and variation in PO in relation to gender, life stages, seasonality, and across different host species.
References
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Journal ArticleDOI
Phylogenetic Perspectives in Innate Immunity
TL;DR: In addition to its role in the early phase of defense, innate immunity in mammals appears to play a key role in stimulating the subsequent, clonal response of adaptive immunity.
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Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor
TL;DR: A family of peptides with broad-spectrum antimicrobial activity has been isolated from the skin of the African clawed frog Xenopus laevis and appears to represent a previously unrecognized class of vertebrate antimicrobial activities.
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Hepcidin, a Urinary Antimicrobial Peptide Synthesized in the Liver *
TL;DR: Hepcidin may be a vertebrate counterpart of cysteine-rich antimicrobial peptides produced in the fat body of insects and exhibited antifungal activity against Candida albicans, Aspergillus fumigatus, and As pergillus nigerand antibacterial activity against Escherichia coli.
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Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides.
TL;DR: This review, which is focused on the different stages of membrane permeation induced by representatives of amphipathic alpha-helical antimicrobial and cell non-selective lytic peptides distinguishes between the 'carpet' mechanism, which holds for antimicrobial peptides versus the 'barrel-stave' mechanisms, which hold for cellnon- selective lytics peptides.
Journal ArticleDOI
The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation
Gaël Nicolas,Caroline Chauvet,Lydie Viatte,Jean Louis Danan,Xavier Bigard,Isabelle Devaux,Carole Beaumont,Axel Kahn,Sophie Vaulont +8 more
TL;DR: Modifications of hepcidin gene expression suggest a key role for hepciridin in iron homeostasis under various pathophysiological conditions, which may support the pharmaceutical use of hePCidin agonists and antagonists in various ironHomeostasis disorders.