Defensins: antifungal lessons from eukaryotes

Silva, Patrı́cia M.R. e; Gonçalves, Sónia; Santos, Nuno C.

doi:10.3389/fmicb.2014.00097

Cited by 102 publications

(82 citation statements)

References 222 publications

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“…To date more than 2200 natural or synthetic AMPs have been reported through the antimicrobial peptide database (APD) (Silva et al 2014). Antimicrobial peptides (AMPs) are generally composed of short sequences of 10–100 amino acids residues and highly amphipathic and membrane active (Reddy et al 2004).…”

Section: Introductionmentioning

confidence: 99%

Antimicrobial activity and stability of the d-amino acid substituted derivatives of antimicrobial peptide polybia-MPI

et al. 2016

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Antimicrobial peptide has the potential to be developed as new kind of antimicrobial agents with novel action mechanism. However, the susceptibility to protease is a drawback for potential peptides to be clinical used. d-amino acid substitution can be one way to increase the proteolytic stability of peptides. In the present study, we synthesized the d-lysines substituted analog (d-lys-MPI) and the d-enantiomer of polybia-MPI (D-MPI) to improve the proteolytic resistance of polybia-MPI. Our results showed that, the stability of its d-amino acid partially substituted analog d-lys-MPI was increased. However, it lost antimicrobial activity at the tested concentration with the loss of α-helix content. As shown in the CD spectra, after substitution, the spectra of D-MPI is symmetrical to MPI, indicated it turned into left hand α-helical conformation. Excitingly, the stability of D-MPI toward the tested protease was improved greatly. Notably, the antimicrobial activity of D-MPI was comparable to its L-counterpart MPI, even improved. In addition, the hemolytic activity of D-MPI was lowered. This also indicated that the action target of antimicrobial peptide polybia-MPI was not chiral specific. So, D-MPI may offer a therapeutic strategy to defend the infection of microbes, considering its stability to protease and relatively lower cytotoxicity to human erythrocytes.

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Section: Introductionmentioning

confidence: 99%

Antimicrobial activity and stability of the d-amino acid substituted derivatives of antimicrobial peptide polybia-MPI

et al. 2016

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“…Antimicrobial peptides (AMPs) have been found in all living things and deeply studied in prokaryotic (4) and eukaryotic cells (5,6). AMPs were shown to play important roles in host innate defense (7,8).…”

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confidence: 99%

Ultrashort Antimicrobial Peptides with Antiendotoxin Properties

Chih

Lin

Yip

et al. 2015

Antimicrob Agents Chemother

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bRelease of lipopolysaccharide (LPS) (endotoxin) from bacteria into the bloodstream may cause serious unwanted stimulation of the host immune system. Some but not all antimicrobial peptides can neutralize LPS-stimulated proinflammatory responses. Salt resistance and serum stability of short antimicrobial peptides can be boosted by adding ␤-naphthylalanine to their termini. Herein, significant antiendotoxin effects were observed in vitro and in vivo with the ␤-naphthylalanine end-tagged variants of the short antimicrobial peptides S1 and KWWK.

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“…and Cryptococcus neoformans. Most of these peptides did not show haemolytic activity against human erythrocytes [51].…”

Section: Action Of Peptides To Treat Fungal Infectionsmentioning

confidence: 91%

Utilisation of peptides against microbial infections – a review

Mirski

Niemcewicz

Bartoszcze

et al. 2017

Ann Agric Environ Med.

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The emergence of resistance in microorganisms on a global scale has made it necessary to search for new antimicrobial factors. Antimicrobial peptides (AMPs) seem to meet these expectations. AMPs are produced by bacteria, viruses, plants, and animals, and may be considered as a new class of drugs intended for the prophylaxis and treatment of both systemic and topical infections. The aim of this study is to review the results of studies on the use of peptides to combat infections in vivo. Antimicrobial peptides may be applied topically and systemically. Among the peptides used topically, a very important area for their application is ophthalmology. AMPs in ophthalmology may be used mainly for the protection of contact lenses from ocular pathogens. Many AMPs are in clinical trials for application in the therapy of local infections. There may be mentioned such preparations as: pexiganan (magainin analogue), MX-226 (based on indolicidin), NEUPREX (isolated from human BPI (bactericidal/permeability-increasing) protein), IB-367 (variant of porcine protegrin), P113 (based on histatin), daptomycin, polymyxins, as well as peptidomimetics. In the combat against systemic infections are used such peptides as: P113D (modified P113 peptide containing D-amino acids), colistin, peptoids, and peptides containing non-typical amino acids or non-peptide elements. AMPs are also used as antiprotozoal, antifungal, antitoxic and immunostimulatory agents. The limitations in the use of peptides in the treatment of infections, such as susceptibility to proteolysis, and resistance of microorganisms to the peptides, are also discussed. AMPs are a promising strategy in the fight against microbial infections.

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Defensins: antifungal lessons from eukaryotes

Cited by 102 publications

References 222 publications

Antimicrobial activity and stability of the d-amino acid substituted derivatives of antimicrobial peptide polybia-MPI

Antimicrobial activity and stability of the d-amino acid substituted derivatives of antimicrobial peptide polybia-MPI

Ultrashort Antimicrobial Peptides with Antiendotoxin Properties

Utilisation of peptides against microbial infections – a review

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