Antimicrobial activity of synthetic all-D mastoparan M.

@article{Li2000AntimicrobialAO,
  title={Antimicrobial activity of synthetic all-D mastoparan M.},
  author={M L Li and Rui-Wen Liao and J W Qiu and Z J Wang and T M Wu},
  journal={International journal of antimicrobial agents},
  year={2000},
  volume={13 3},
  pages={
          203-8
        }
}
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30 Citations
Background Citations
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Methods Citations
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30 Citations

Citation Type

Citation Type

Structural and biological characterization of mastoparans in the venom of Vespa species in Taiwan
The structure and antimicrobial potential of wasp and hornet (Vespidae) mastoparans: A review
TLDR
All tested hornet mastoparans have strong antimicrobial activities, suggesting that they can provide useful insights into and opportunities for development of novel antibacterial peptides.
A synthesized cationic tetradecapeptide from hornet venom kills bacteria and neutralizes lipopolysaccharide in vivo and in vitro.
Selective amino acid substitution reduces cytotoxicity of the antimicrobial peptide mastoparan.
Structural and functional characterization of two novel peptide toxins isolated from the venom of the social wasp Polybia paulista
Exploración estructural de perfiles de actividad antibacteriana y hemolítica de análogos no naturales del péptido antimicrobiano Mastoparán MP-8
TLDR
The relevance of a systematic replacement of peptide-bonds on the Mastoparan MP-8 antimicrobial peptide to afford 27 new pseudopeptide analogues is reported and all obtained molecules possess a high stability profile when tested against a severe proteolytic attack.
In vitro activity of mastoparan-AF alone and in combination with clinically used antibiotics against multiple-antibiotic-resistant Escherichia coli isolates from animals
Evaluating antioxidative activities of amino acid substitutions on mastoparan-B
Wasp Venom Biochemical Components and Their Potential in Biological Applications and Nanotechnological Interventions
TLDR
Wasp venom could be a potential and novel natural source to develop innovative pharmaceuticals and new agents for drug discovery.
D-form KLKLLLLLKLK-NH2 peptide exerts higher antimicrobial properties than its L-form counterpart via an association with bacterial cell wall components
TLDR
The results indicate that the D-form KLKLLLLLkLKLK-NH2 peptide has higher antimicrobial activity than the L-form via a specific association with bacterial cell wall components, including peptidoglycan.
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References

SHOWING 1-10 OF 25 REFERENCES
Interaction of mastoparan‐B from venom of a hornet in taiwan with phospholipid bilayers and its antimicrobial activity
TLDR
The difference in the hydrophilic surface area on the molecules seems to lead to the subtle change in its interaction with membranes, resulting in the alteration of biological activity.
Mastoparan B, synthesis and its physical and biological properties.
TLDR
Mastoparan B, a tetradecapeptide toxin isolated from the hornet (Vespa basalis) venom, was synthesized chemically and found to have a potent antibacterial activity to both Gram negative and Gram positive bacteria.
Facilitation of phospholipase A2 activity by mastoparans, a new class of mast cell degranulating peptides from wasp venom.
Mastoparan, a peptide toxin from wasp venom, mimics receptors by activating GTP-binding regulatory proteins (G proteins).
Antibacterial and antimalarial properties of peptides that are cecropin‐melittin hybrids
Interactions between membranes and cytolytic peptides.
All-D amino acid-containing channel-forming antibiotic peptides.
TLDR
The D enantiomers of three naturally occurring antibiotics--cecropin A, magainin 2 amide, and melittin--were synthesized and it is suggested that the mode of action of these peptides on the membranes of bacteria, erythrocytes, plasmodia, and artificial lipid bilayers may be similar and involves the formation of ion-channel pores spanning the membranes, but without specific interaction with chiral receptors or enzymes.
Regulation of Gi and Go by mastoparan, related amphiphilic peptides, and hydrophobic amines. Mechanism and structural determinants of activity.
Phospholipases: melittin facilitation of bee venom phospholipase A2-catalyzed hydrolysis of unsonicated lecithin liposomes.
Membrane interactions of mastoparan analogues related to their differential effects on protein kinase C, Na,K‐ATPase and HL60 cells
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