Three Valuable Peptides from Bee and Wasp Venoms for Therapeutic and Biotechnological Use:  Melittin, Apamin and Mastoparan

Moreno, Miguel; Giralt, Ernest

doi:10.3390/toxins7041126

Cited by 289 publications

(297 citation statements)

References 161 publications

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“…6,7 Both of these enzymes are classified as major allergens according to the International Union of Immunological Societies, as they are capable of inducing the IgE response in susceptible individuals. [6][7][8] The results of study confirm that a high purity and recovery yield of melittin can be obtained with a one-step purification method with strong cationexchange chromatography resins using sodium phosphate buffer at pH 6. The optimal step-wise elution condition was designed to increase the yield and concentration of the melittin collected.…”

Section: Introductionmentioning

confidence: 99%

Isolation and Identification of Biologically Active Components from the Honey Bee Venom Apis Mellifera L. Caucasica

Fz¹,

ShA²

2017

MOJT

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The article presents experimental data on the separation and identification of biologically active components of the venom of the honey bee Apis mellifera L. Caucasica. By gel chromatography on a column with Servacel-52 eluting with a linear gradient of NaCl concentration from 0.01 to 1M, followed by spectrophotometric measurement of the unit of optical density at an absorption wavelength of λ=280nm on a Hitachi-557 spectrophotometer from the honey bee venom, biologically active components of zootoxin with molecular weights of 12000, 14600 and 22000D. A polypeptide with Mg~12000D is a toxic component identified as mellitine, a polypeptide with Mg~14600 is an enzyme of phospholipase A2, and a polypeptide with Mg~22000D is a glycoprotein.

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Section: Introductionmentioning

confidence: 99%

Isolation and Identification of Biologically Active Components from the Honey Bee Venom Apis Mellifera L. Caucasica

Fz¹,

ShA²

2017

MOJT

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“…Bee venom consists mainly of melittin (approximately 40-50%) as well as small quantities of polypeptides and low molecular compounds 23) ; the bee venom used in this study contained 56.7% melittin. Melittin has a variety of biological activities 27,28) including proliferative effects on hDPCs and growth factor stimulation. Although we could not clearly explain that melittin is the active main component, melittin might play some role as a hair growth-promoting component in bee venom.…”

Section: Discussionmentioning

confidence: 99%

Bee Venom Promotes Hair Growth in Association with Inhibiting 5α-Reductase Expression

Park

Erdogan

Hwang

et al. 2016

Biological & Pharmaceutical Bulletin

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Alopecia is an important issue that can occur in people of all ages. Recent studies show that bee venom can be used to treat certain diseases including rheumatoid arthritis, neuralgia, and multiple sclerosis. In this study, we investigated the preventive effect of bee venom on alopecia, which was measured by applying bee venom (0.001, 0.005, 0.01%) or minoxidil (2%) as a positive control to the dorsal skin of female C57BL/6 mice for 19 d. Growth factors responsible for hair growth were analyzed by quantitative real-time PCR and Western blot analysis using mice skins and human dermal papilla cells (hDPCs). Bee venom promoted hair growth and inhibited transition from the anagen to catagen phase. In both anagen phase mice and dexamethasone-induced catagen phase mice, hair growth was increased dose dependently compared with controls. Bee venom inhibited the expression of SRD5A2, which encodes a type II 5α-reductase that plays a major role in the conversion of testosterone into dihydrotestosterone. Moreover, bee venom stimulated proliferation of hDPCs and several growth factors (insulin-like growth factor 1 receptor (IGF-1R), vascular endothelial growth factor (VEGF), fibroblast growth factor (FGF)2 and 7) in bee venom-treated hDPCs dose dependently compared with the control group. In conclusion, bee venom is a potentially potent 5α-reductase inhibitor and hair growth promoter.

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“…Peptide based drugs find interest because of their high specificity to their target and high activity compared to small molecule drugs [2]. Furthermore, with the cargo carrying properties of CPPs, they are finding use in the delivery of cancer drugs such as doxorubicin [248,355], taxol [356], paclitaxel [357], docetaxel [358].…”

Section: Future Perspectives: Characterizing Membrane Active Peptidesmentioning

confidence: 99%

“…The field of AMPs is especially more intense due to the urgent need for novel antimicrobials, with more than 600 articles published in 2017 ( Figure 1). In contrast to antimicrobials that target proteins, cells cannot readily build resistance to AMPs that target the cell membrane because it is difficult, if not impossible, to alter this crucial cell structure [2]. AMPs have been shown to have antiviral [3] and anticancer [4] activities as well.…”

Section: Introductionmentioning

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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Three Valuable Peptides from Bee and Wasp Venoms for Therapeutic and Biotechnological Use: Melittin, Apamin and Mastoparan

Cited by 289 publications

References 161 publications

Isolation and Identification of Biologically Active Components from the Honey Bee Venom Apis Mellifera L. Caucasica

Isolation and Identification of Biologically Active Components from the Honey Bee Venom Apis Mellifera L. Caucasica

Bee Venom Promotes Hair Growth in Association with Inhibiting 5α-Reductase Expression

Membrane Active Peptides and Their Biophysical Characterization

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