Melittin peptides exhibit different activity on different cells and model membranes

Jamasbi, Elaheh; Batinovic, Steven; Sharples, Robyn A.; Sani, Marc‐Antoine; Robins-Browne, Roy M.; Wade, John D.; Separovic, Frances; Hossain, Mohammed Akhter

doi:10.1007/s00726-014-1833-9

Cited by 65 publications

(58 citation statements)

References 51 publications

(44 reference statements)

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“…Such preference was suggested to correlate with higher amount of negatively charged lipids in Gram-positive when compared with Gram-negative bacteria (24). Mac1 is less efficient in inhibiting the growth of bacteria than the bee venom peptide melittin, also known for its antimicrobial activity (25), with the latter inhibiting bacterial growth at 2 and 0.5 M against E. coli and S. aureus, respectively (Table 1). Notably, a 4-fold greater potency against Gram-positive was also observed.…”

Section: Mac1 Has Antimicrobial Activity Against S Aureus and E Colmentioning

confidence: 99%

“…Mac1 and melittin have been used in many experiments without showing any solubility or secondary structure perturbations in buffer with up to 150 mM NaCl (14,15,25). Therefore, it may be that bacteria are able to withstand harsh membrane damage in high salt (LB) compared with low salt growth medium (MHB).…”

Section: Mac1 Has Antimicrobial Activity Against S Aureus and E Colmentioning

confidence: 99%

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Bacteria May Cope Differently from Similar Membrane Damage Caused by the Australian Tree Frog Antimicrobial Peptide Maculatin 1.1

Sani

Henriques

Weber

et al. 2015

Journal of Biological Chemistry

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Background: Mac1 specificity and bactericidal concentrations may be due to a distinctive membrane disrupting mechanism. Results: S. aureus growth is inhibited at 16-fold lower Mac1 concentration than E. coli, but both lipid membranes are compromised at similar concentrations. Conclusion: Bacteria may cope differently with membrane damage. Significance: Antimicrobial peptide mode of action needs to be better understood to develop new drug candidate.

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Section: Mac1 Has Antimicrobial Activity Against S Aureus and E Colmentioning

confidence: 99%

Section: Mac1 Has Antimicrobial Activity Against S Aureus and E Colmentioning

confidence: 99%

Bacteria May Cope Differently from Similar Membrane Damage Caused by the Australian Tree Frog Antimicrobial Peptide Maculatin 1.1

Sani

Henriques

Weber

et al. 2015

Journal of Biological Chemistry

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“…Topical cosmetic products containing bee venom are gaining popularity for the treatment of acne and skin diseases. However, the cytotoxicity of melittin limits the amount of melittin that can be used in cosmetic formulations (Han et al, 2013;Jamasbi et al, 2014). Commercial cosmetic products compromise cytotoxicity simply by reducing the amount of melittin which also leads to an input cost reduction.…”

Section: Discussionmentioning

confidence: 99%

“…The anti-microbial and anti-inflammatory activities of melittin have raised a commercial interest in treating bacteria-caused skin problems and diseases. However, great care needs to be taken over the amount incorporated into commercial products due to the cytotoxicity of melittin (Jamasbi et al, 2014). Reliable quantification assays are needed for melittin which specify the endogenous levels in bee venom, and which specify the supplemental levels of melittin used in cosmetic formulations.…”

Section: Melittin Quantification By Elisamentioning

confidence: 99%

The Use of Chicken Igy in a Double Antibody Sandwich Elisa for the Quantification of Melittin in Bee Venom and Bee Venom Melittin Content in Cosmetics

Suh

Kartoon

Gujral

et al. 2015

Journal of Apicultural Science

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A b s t r a c t Two enzyme-linked immunosorbent assay (ELISA) -based detection systems: indirect competitive ELISA and biotinylated double antibody sandwich ELISA (DAS-ELISA) were developed to determine the melittin concentration in honeybee (Apis mellifera) venom and the melittin concentration in cosmetics which contain bee venom. The indirect competitive ELISA employed chicken anti-melittin IgY. The biotinylated DAS-ELISA employed anti-melittin monoclonal antibody (MAb) and biotinylated anti-melittin IgY. To produce anti-melittin IgY; Sigma melittin was emulsified with Freund's incomplete adjuvant and immunised to Leghorn laying chickens intramuscularly at four different sites (50 µg/mL, 0.25 mL per site) of the breast muscles. After 5 to 8 weeks of the immunisation, anti-melittin IgY was extracted and analysed by ELISA. The anti-melittin IgY antibody produced was highly specific to melittin and did not cross-react with other bee venom proteins, as examined by ELISA and a western-blot assay. Indirect competitive ELISA demonstrated a higher range of melittin detection (2.5 to 80 µg/mL). Double antibody sandwich ELISA using MAb as the capture antibody and biotinylated polyclonal IgY as the detection antibody, provided a lower range of detection (2.5 -40 ng/mL), which has a 1000 times higher sensitivity than that of indirect competitive ELISA. Therefore, indirect competitive ELISA is a useful tool to measure the concentration of melittin in bee venom as a raw material. Biotinylated DAS-ELISA, on the other hand, is more suitable for nanoscale quantification of melittin in commercial products.

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“…Melittin, a 26 residue cationic amphipathic peptide with the sequence GIGAVLKVLTTGLPALISWIKRKRQQ, is the principal toxic component of bee venom [16] with antimicrobial, antiviral, antifungal, anticancer [319], and anti-inflammatory properties [74,320]. The melittin monomer can be divided into three regions: 1.…”

Section: Melittinmentioning

confidence: 99%

Membrane Active Peptides and Their Biophysical Characterization

Avcı

Akbulut

Özkırımlı

2018

Preprint

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In the last 20 years, an increasing number of studies have been reported on membrane active peptides, which exert their biological activity by interacting with the cell membrane either to disrupt it and lead to cell lysis or to translocate through it to deliver cargos into the cell and reach their target. These peptides are attractive alternatives to currently used pharmaceuticals. Antimicrobial peptides (AMPs) and peptides designed for drug and gene delivery currently in the drug pipeline suggest that these membrane active peptides will soon constitute a significant percentage of the drug market. Here, we focus on two most prominent classes of membrane active peptides; AMPs and cell-penetrating peptides (CPPs). AMPs are a group of membrane active peptides that disrupt the membrane integrity or inhibit the cellular functions of bacteria, virus and fungi. CPPs are another group of membrane active peptides that mainly function as cargo-carriers even though they may also show antimicrobial activity to some extent. Biophysical techniques to understand how they interact with the membrane have shed light on the peptide-membrane interaction at various levels of detail. Structural investigation of membrane active peptides in the presence of the membrane provides important clues on the effect of the membrane environment on peptide conformations. Advances in live imaging techniques have allowed examination of peptide action at a single cell or single molecule level. In addition to these experimental biophysical techniques, molecular dynamics simulations provided clues on the peptide-lipid interactions and dynamics of the cell entry process at atomic detail. In this review, we summarize the recent advances in experimental and computational investigation of membrane active peptides with particular emphasis on two amphipathic membrane active peptides, the AMP melittin and the CPP pVEC.

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Melittin peptides exhibit different activity on different cells and model membranes

Cited by 65 publications

References 51 publications

Bacteria May Cope Differently from Similar Membrane Damage Caused by the Australian Tree Frog Antimicrobial Peptide Maculatin 1.1

Bacteria May Cope Differently from Similar Membrane Damage Caused by the Australian Tree Frog Antimicrobial Peptide Maculatin 1.1

The Use of Chicken Igy in a Double Antibody Sandwich Elisa for the Quantification of Melittin in Bee Venom and Bee Venom Melittin Content in Cosmetics

Membrane Active Peptides and Their Biophysical Characterization

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