Antimicrobial Peptides: Their History, Evolution, and Functional Promiscuity

doi:10.1002/9783527652853.ch1

Cited by 30 publications

(9 citation statements)

References 317 publications

(220 reference statements)

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“…A variety of resistance mechanisms to AMPs have been described in bacteria, which generally involve the inherent properties of these organisms rather than the acquisition of dedicated resistance genes 13 . This intrinsic protection from AMPs is generally moderate in level and relatively non-specific in nature, which is reflected in the low frequency of resistant bacteria and the evolutionary persistence and success of these peptides 14 . The evolution of bacterial resistance to AMPs has been demonstrated experimentally 15 , but based on the pharmacodynamics of these peptides, it has been predicted that they are much less likely to select for resistant mutants in vivo than conventional antibiotics 16 .…”

Section: Introductionmentioning

confidence: 99%

Biophysical investigation into the antibacterial action of modelin-5-NH₂

Dennison

Hauß

Badiani³

et al. 2019

Soft Matter

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Section: Introductionmentioning

confidence: 99%

Biophysical investigation into the antibacterial action of modelin-5-NH₂

Dennison

Hauß

Badiani³

et al. 2019

Soft Matter

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“…Although AMPs have been known since 1939 [15] (i.e., the first isolated peptides were gramicidins from the soil bacteria Aneurinibacillus migulanus), it was not until 1981 that the first insect antimicrobial peptide, named cecropin, was identified from the hemolymph of the Hyalophora cecropia pupae [59,60]. Several AMPs that can be classified according to their structure or function in different families (such as cecropins, ponericins, defensins, lebocins, drosocin, Metchnikowin, gloverins, diptericins and attacins) are presently known in insects.…”

Section: Insects Antimicrobial Peptides: a Brief Insightmentioning

confidence: 99%

“…Since AMPs most likely derive from multiple independent evolutionary events, these molecules display an astounding diversity among taxa [2,15,16], but, at the same time, they share some common physicochemical properties that allow their classification into broad categories.…”

Section: Introductionmentioning

confidence: 99%

Attacins: A Promising Class of Insect Antimicrobial Peptides

et al. 2021

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Insects produce a large repertoire of antimicrobial peptides (AMPs) as the first line of defense against bacteria, viruses, fungi or parasites. These peptides are produced from a large precursor that contains a signal domain, which is cleaved in vivo to produce the mature protein with antimicrobial activity. At present, AMPs from insects include several families which can be classified as cecropins, ponericins, defensins, lebocins, drosocin, Metchnikowin, gloverins, diptericins and attacins according to their structure and/or function. This short review is focused on attacins, a class of glycine-rich peptides/proteins that have been first discovered in the cecropia moth (Hyalophora cecropia). They are a rather heterogeneous group of immunity-related proteins that exhibit an antimicrobial effect mainly against Gram-negative bacteria. Here, we discuss different attacin and attacin-like AMPs that have been discovered so far and analyze their structure and phylogeny. Special focus is given to the physiological importance and mechanism of action of attacins against microbial pathogens together with their potential pharmacological applications, emphasizing their roles as antimicrobials.

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“…Peptide focused research has been undertaken for over 100 years, concentrating particularly on neuropeptides and peptides with various bioactivities (e.g., antimicrobial, cell penetrating and ACE-inhibition). Until recently, the high throughput study of peptidomes was not achievable and as such endogenous proteolytic events occurring in peptidomes of interest remained largely unexplored.…”

Section: Introductionmentioning

confidence: 99%

Peptigram: A Web-Based Application for Peptidomics Data Visualization

et al. 2016

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Tandem mass spectrometry (MS/MS) techniques, developed for protein identification, are increasingly being applied in the field of peptidomics. Using this approach, the set of protein fragments observed in a sample of interest can be determined to gain insights into important biological processes such as signaling and other bioactivities. As the peptidomics era progresses, there is a need for robust and convenient methods to inspect and analyze MS/MS derived data. Here, we present Peptigram, a novel tool dedicated to the visualization and comparison of peptides detected by MS/MS. The principal advantage of Peptigram is that it provides visualizations at both the protein and peptide level, allowing users to simultaneously visualize the peptide distributions of one or more samples of interest, mapped to their parent proteins. In this way rapid comparisons between samples can be made in terms of their peptide coverage and abundance. Moreover, Peptigram integrates and displays key sequence features from external databases and links with peptide analysis tools to offer the user a comprehensive peptide discovery resource. Here, we illustrate the use of Peptigram on a data set of milk hydrolysates. For convenience, Peptigram is implemented as a web application, and is freely available for academic use at http://bioware.ucd.ie/peptigram .

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Antimicrobial Peptides: Their History, Evolution, and Functional Promiscuity

Cited by 30 publications

References 317 publications

Biophysical investigation into the antibacterial action of modelin-5-NH₂

Biophysical investigation into the antibacterial action of modelin-5-NH₂

Attacins: A Promising Class of Insect Antimicrobial Peptides

Peptigram: A Web-Based Application for Peptidomics Data Visualization

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Antimicrobial Peptides: Their History, Evolution, and Functional Promiscuity

Cited by 30 publications

References 317 publications

Biophysical investigation into the antibacterial action of modelin-5-NH2

Biophysical investigation into the antibacterial action of modelin-5-NH2

Attacins: A Promising Class of Insect Antimicrobial Peptides

Peptigram: A Web-Based Application for Peptidomics Data Visualization

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Biophysical investigation into the antibacterial action of modelin-5-NH₂

Biophysical investigation into the antibacterial action of modelin-5-NH₂