Dual antifungal properties of cationic antimicrobial peptides polybia-MPI: Membrane integrity disruption and inhibition of biofilm formation

Wang, Kairong; Yan, Jiexi; Wen, Dandan; Xie, Junqiu; Yan, Bo; Yan, Wenjin; Sun, Mengyang; Zhang, Bangzhi; Ma, Mingxia; Zhao, Yanyan; Jia, Fengjing; Zhu, Ranran; Chen, Wei; Wang, Rui

doi:10.1016/j.peptides.2014.03.005

Cited by 56 publications

(40 citation statements)

References 24 publications

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“…Membrane active action mode of AMPs was believed that it is difficult for microbes to develop resistance toward AMPs (Hancock and Sahl 2006). The L-counterpart of D-MPI mainly exerts its antitumor, antibacterial and antifungal activity through the disruption of the integrity of cell membrane (Wang et al 2008, 2009, 2013, 2014). As expected, it may also exert its antimicrobial activity through disrupting the integrity of cell membrane and lead to the death of cells.…”

Section: Discussionmentioning

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: Discussionmentioning

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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“…A bacterial membrane permeability assay was conducted as described previously (Wang et al, 2014). A total of 200 μl bacterial suspension (1×10 8 CFU/ml) was incubated with HMGN2 or bovine serum albumin (BSA, 5 μg/ml) at 37 °C for 240 min.…”

Section: Bacterial Membrane Permeability Testmentioning

confidence: 99%

Antibacterial mechanism of high-mobility group nucleosomal-binding domain 2 on the Gram-negative bacteria Escherichia coli

Shen

Zhou

et al. 2017

J. Zhejiang Univ. Sci. B

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“…Polybia-MP-I [145] and Polybia-CP [146] also inhibits fungal cells growth. Both venom peptides have shown a significantly antifungal and fungicidal activity against different species of Candida.…”

Section: Antimicrobial and Antifungal Activitymentioning

confidence: 97%

Wasp venomic: Unravelling the toxins arsenal of Polybia paulista venom and its potential pharmaceutical applications

Pérez-Riverol

Santos-Pinto

Lasa

et al. 2017

Journal of Proteomics

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Polybia paulista (Hymenoptera: Vespidae) is a neotropical social wasp from southeast Brazil. As most social Hymenoptera, venom from P. paulista comprises a complex mixture of bioactive toxins ranging from low molecular weight compounds to peptides and proteins. Several efforts have been made to elucidate the molecular composition of the P. paulista venom. Data derived from proteomic, peptidomic and allergomic analyses has enhanced our understanding of the whole envenoming process caused by the insect sting. The combined use of bioinformatics, -omics- and molecular biology tools have allowed the identification, characterization, in vitro synthesis and recombinant expression of several wasp venom toxins. Some of these P. paulista - derived bioactive compounds have been evaluated for the rational design of antivenoms and the improvement of allergy specific diagnosis and immunotherapy. Molecular characterization of crude venom extract has enabled the description and isolation of novel toxins with potential biotechnological applications. Here, we review the different approaches that have been used to unravel the venom composition of P. paulista. We also describe the main groups of P. paulista - venom toxins currently identified and analyze their potential in the development of component-resolved diagnosis of allergy, and in the rational design of antivenoms and novel bioactive drugs.

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Dual antifungal properties of cationic antimicrobial peptides polybia-MPI: Membrane integrity disruption and inhibition of biofilm formation

Cited by 56 publications

References 24 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

Antibacterial mechanism of high-mobility group nucleosomal-binding domain 2 on the Gram-negative bacteria Escherichia coli

Wasp venomic: Unravelling the toxins arsenal of Polybia paulista venom and its potential pharmaceutical applications

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