Antitumor effects, cell selectivity and structure–activity relationship of a novel antimicrobial peptide polybia-MPI

Wang, Kairong; Zhang, Bangzhi; Zhang, Wei; Yan, Jiexi; Li, Jia; Wang, Rui

doi:10.1016/j.peptides.2008.01.015

Cited by 139 publications

(98 citation statements)

References 17 publications

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“…Circular dichroism (CD) was performed as described previously (11). Briefly, CD spectra of peptides were recorded using a CD spectrophotometer (Olis DSM 1000) nitrogen flushing in a 1-mm-path-length cell at 25°C.…”

Section: Methodsmentioning

confidence: 99%

Membrane Perturbation Action Mode and Structure-Activity Relationships of Protonectin, a Novel Antimicrobial Peptide from the Venom of the Neotropical Social Wasp Agelaia pallipes pallipes

Wang

Wen

Yan

et al. 2013

Antimicrob Agents Chemother

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With the extensive use of antibiotics, multidrug-resistant bacteria emerge frequently. New antimicrobial agents with novel modes of action are urgently needed. It is now widely accepted that antimicrobial peptides (AMPs) could be promising alternatives to conventional antibiotics. In this study, we aimed to study the antimicrobial activity and mechanism of action of protonectin, a cationic peptide from the venom of the neotropical social wasp Agelaia pallipes pallipes. We demonstrated that protonectin exhibits potent antimicrobial activity against a spectrum of bacteria, including multidrug-resistant strains. To further understand this mechanism, the structural features of protonectin and its analogs were studied by circular dichroism (CD). The CD spectra demonstrated that protonectin and its natural analog polybia-CP formed a typical ␣-helical conformation in the membrane-mimicking environment, while its proline-substituted analog had much lower or even no ␣-helix conformation. Molecular dynamics simulations indicated that the ␣-helical conformation in the membrane is required for the exhibition of antibacterial activity. In conclusion, protonectin exhibits potent antimicrobial activity by disruption of the integrity of the bacterial membrane, and its ␣-helical confirmation in the membrane is essential for this action.

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Section: Methodsmentioning

confidence: 99%

Membrane Perturbation Action Mode and Structure-Activity Relationships of Protonectin, a Novel Antimicrobial Peptide from the Venom of the Neotropical Social Wasp Agelaia pallipes pallipes

Wang

Wen

Yan

et al. 2013

Antimicrob Agents Chemother

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“…It may therefore be expected that the composition of the lipid bilayer will play an important role in peptide action. In addition to potent and broad-spectrum bactericide activity, the peptide Polybia-MP-1 (MP1) also inhibited the proliferation of prostate and bladder cancer cells (Wang et al 2008) and, in lymphocytes, proved to be multidrug resistant ). It was observed that this peptide selectively recognized leukemic T-lymphocytes and not healthy ones, being harmful only to leukemic ones (Dos Santos Cabrera et al 2012).…”

Section: The Effect Of Lipid Composition On Affinity and Lytic Activimentioning

confidence: 99%

Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides

2017

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The indiscriminate use of conventional antibiotics is leading to an increase in the number of resistant bacterial strains, motivating the search for new compounds to overcome this challenging problem. Antimicrobial peptides, acting only in the lipid phase of membranes without requiring specific membrane receptors as do conventional antibiotics, have shown great potential as possible substituents of these drugs. These peptides are in general rich in basic and hydrophobic residues forming an amphipathic structure when in contact with membranes. The outer leaflet of the prokaryotic cell membrane is rich in anionic lipids, while the surface of the eukaryotic cell is zwitterionic. Due to their positive net charge, many of these peptides are selective to the prokaryotic membrane. Notwithstanding this preference for anionic membranes, some of them can also act on neutral ones, hampering their therapeutic use. In addition to the electrostatic interaction driving peptide adsorption by the membrane, the ability of the peptide to perturb lipid packing is of paramount importance in their capacity to induce cell lysis, which is strongly dependent on electrostatic and hydrophobic interactions. In the present research, we revised the adsorption of antimicrobial peptides by model membranes as well as the perturbation that they induce in lipid packing. In particular, we focused on some peptides that have simultaneously acidic and basic residues. The net charges of these peptides are modulated by pH changes and the lipid composition of model membranes. We discuss the experimental approaches used to explore these aspects of lipid membranes using lipid vesicles and lipid monolayer as model membranes.

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“…According to the APD [9], more than a dozen of peptides have been expressed in plants to reduce or avoid infection. In addition, lactoferricin, distinctin, ranalexin, halocidin, polybia-MPI, chicken cathelicidin 1 (fowlicidin-1), bacterial mutacin B-Ny266, and bacterial ABP-118 have been tested in mice models [73][74][75][76][77][78][79][80]. Other engineered peptides or AMP mimics that have been evaluated in animal models include D, L-peptides, WLBU2, Pro-rich A3-APO, and acyl-lysyl oligomers [81][82][83][84].…”

Section: Therapeutic Potentials Of Ampsmentioning

confidence: 99%

“…Some of the post-translational strategies, such as C-terminal amidation, cyclization, D-amino acid incorporation, and halogenation, have been adopted in laboratories to enhance peptide stability to proteases. As a consequence, several engineered peptides have been demonstrated to be able to keep animal healthy [73][74][75][76][77][78][79][80][81][82][83][84].…”

Section: Concluding Remarks and Future Directionsmentioning

confidence: 99%

Post-Translational Modifications of Natural Antimicrobial Peptides and Strategies for Peptide Engineering

Wang¹

2011

CBIOT

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Natural antimicrobial peptides (AMPs) are gene-coded defense molecules discovered in all the three life domains: Eubacteria, Archaea, and Eukarya. The latter covers protists, fungi, plants, and animals. It is now recognized that amino acid composition, peptide sequence, and posttranslational modifications determine to a large extent the structure and function of AMPs. This article systematically describes post-translational modifications of natural AMPs annotated in the antimicrobial peptide database (http://aps.unmc.edu/AP). Currently, 1147 out of 1755 AMPs in the database are modified and classified into more than 17 types. Through chemical modifications, the peptides fold into a variety of structural scaffolds that target bacterial surfaces or molecules within cells. Chemical modifications also confer desired functions to a particular peptide. Meanwhile, these modifications modulate other peptide properties such as stability. Elucidation of the relationship between AMP property and chemical modification inspires peptide engineering. Depending on the objective of our design, peptides may be modified in various ways so that the desired features can be enhanced whereas unwanted properties can be minimized. Therefore, peptide design plays an essential role in developing natural AMPs into a new generation of therapeutic molecules.

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Antitumor effects, cell selectivity and structure–activity relationship of a novel antimicrobial peptide polybia-MPI

Cited by 139 publications

References 17 publications

Membrane Perturbation Action Mode and Structure-Activity Relationships of Protonectin, a Novel Antimicrobial Peptide from the Venom of the Neotropical Social Wasp Agelaia pallipes pallipes

Membrane Perturbation Action Mode and Structure-Activity Relationships of Protonectin, a Novel Antimicrobial Peptide from the Venom of the Neotropical Social Wasp Agelaia pallipes pallipes

Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides

Post-Translational Modifications of Natural Antimicrobial Peptides and Strategies for Peptide Engineering

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