�ber die Struktur des toxischen Bienengiftpeptids Melittin und deren Beziehung zur pharmakologischen Wirkung

Habermann, E.; Jentsch, Joachim

doi:10.1007/bf00259241

Cited by 10 publications

(4 citation statements)

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“…The amino acid sequences of melittin (from reference 20) and the amino acid sequence and helical projection for the melittin analogue, peptide 1. ratio of 2:1 could provide valuable information concerning the role of the hydrophobic-hydrophilic balance in the interaction of amphiphilic peptides with phospholipid mono-and bilayers. For the above reasons we designed the amphiphilic a-helical melittin analogue peptide I, shown in Fig.…”

Section: Figurementioning

confidence: 99%

Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue

DeGrado¹,

Musso²,

Lieber³

et al. 1982

Biophysical Journal

248

172

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The cytotoxic peptide from honeybee venom, melittin, and a synthetic peptide analogue of it lyse human erythrocytes in a biphasic process. The kinetics of the lysis in 0.30 M sucrose, 0.01 M sodium phosphate, pH 7.30 at 4 degrees C were investigated. Our results show that melittin rapidly binds to the outer surface of the erythrocyte membrane, and the surface-bound monomers produce transient openings through which approximately 40 hemoglobin molecules can escape. Concomitantly, the melittin loses its ability to effect the process, presumably by translocation through the bilayer. The half-life for this process is 1.2 min. In a much slower process, dimers of this internalized melittin again produce transient membrane openings in a steady state. On a molar basis, the synthetic peptide analogue produces a fast process comparable to that caused by melittin, but is more efficient in the slow phase. Escape of hemoglobin and of carbonic anhydrase through the openings is diffusion controlled. These results suggest that the functional units necessary for the activity of melittin-like cytotoxic peptides are a 20 amino acid amphiphilic alpha-helix with a hydrophobic:hydrophilic ratio greater than 1 and a short segment with a high concentration of positive charges.

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Section: Figurementioning

confidence: 99%

Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue

DeGrado¹,

Musso²,

Lieber³

et al. 1982

Biophysical Journal

248

172

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“…BV also has numerous polypeptides, the main one being melittin, which is also the main component of BV and has many positive biological effects and a relatively low toxicity. Melittin has a molecular weight of 2,840 Daltons, but it can reach 12,500 Daltons because it can also be in a tetrameric form [ 2 , 3 ].…”

Section: Introductionmentioning

confidence: 99%

Honey Bee Venom (Apis mellifera) Contains Anticoagulation Factors and Increases the Blood-clotting Time

2015

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Objectives:Bee venom (BV) is a complex mixture of proteins and contains proteins such as phospholipase and melittin, which have an effect on blood clotting and blood clots. The mechanism of action of honey bee venom (HBV, Apis mellifera) on human plasma proteins and its anti-thrombotic effect were studied. The purpose of this study was to investigate the anti-coagulation effect of BV and its effects on blood coagulation and purification.Methods:Crude venom obtained from Apis mellifera was selected. The anti-coagulation factor of the crude venom from this species was purified by using gel filtration chromatography (sephadex G-50), and the molecular weights of the anti-coagulants in this venom estimated by using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Blood samples were obtained from 10 rabbits, and the prothrombin time (PT) and the partial thromboplastin time (PTT) tests were conducted. The approximate lethal dose (LD) values of BV were determined.Results:Crude BV increased the blood clotting time. For BV concentrations from 1 to 4 mg/mL, clotting was not observed even at more than 300 seconds, standard deviations (SDs) = ± 0.71; however, clotting was observed in the control group 13.8 s, SDs = ± 0.52. Thus, BV can be considered as containing anti-coagulation factors. Crude BV is composed 4 protein bands with molecular weights of 3, 15, 20 and 41 kilodalton (kDa), respectively. The LD50 of the crude BV was found to be 177.8 μg/mouse.Conclusion:BV contains anti-coagulation factors. The fraction extracted from the Iranian bees contains proteins that are similar to anti-coagulation proteins, such as phospholipase A2 (PLA2) and melittin, and that can increase the blood clotting times in vitro.

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“…Melittin, by weight the principal constituent of the venom (c. 30%) is a peptide of 26 amino acid residues, which has a high surface activity and is a potent haemolysin (Habermann & Jentsch, 1966). Apamin (c. 2% of the venom) contains 18 amino acid residues and is a neurotoxin producing motor abnormalities associated with actions upon the central nervous system (Habermann & Reiz, 1 965a).…”

Section: Introductionmentioning

confidence: 99%

ANTI‐INFLAMMATORY PROPERTY OF 401 (MCD‐PEPTIDE), A PEPTIDE FROM THE VENOM OF THE BEE Apis mellifera (L.)

Hanson

Morley

Soria-Herrera

1974

British J Pharmacology

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Peptide 401, a potent mast cell degranulating factor from bee venom, substantially inhibited the oedema provoked by subplantar injection of carrageenin or intra‐articular injection of turpentine in the rat. The ED50 of 401 was c. 0.1 mg/kg. The anti‐inflammatory effect was assessed by measurement of the increased 125I‐albumin content of an injected site in comparison with an uninjected contralateral site. Peptide 401 also suppressed the increased vascular permeability due to intradermal injection of various smooth muscle spasmogens (histamine, bradykinin, 5‐hydroxytryptamine (5‐HT), and prostaglandins). Other comparable mast cell degranulating agents (48/80 and melittin) showed little evidence of anti‐inflammatory activity when tested at comparable dosage on turpentine arthritis and carrageenin oedema. The anti‐inflammatory effects were not abolished by pretreatment with mepyramine and methysergide, which abolished the increased vascular permeability produced by local injection of 401. The anti‐inflammatory action of 401 was not affected by regional denervation or pretreatment with phenoxybenzamine, and was reduced but not abolished by adrenalectomy. Measurement of skin temperature, fractional extraction of 86Rb and blood flow in perfused mesentery gave no evidence that the anti‐inflammatory action of 401 was due to reduced tissue perfusion. It is concluded that 401 may exert its anti‐inflammatory action directly by making the vascular endothelium anergic to phlogistic stimuli.

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�ber die Struktur des toxischen Bienengiftpeptids Melittin und deren Beziehung zur pharmakologischen Wirkung

Cited by 10 publications

References 0 publications

Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue

Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue

Honey Bee Venom (Apis mellifera) Contains Anticoagulation Factors and Increases the Blood-clotting Time

ANTI‐INFLAMMATORY PROPERTY OF 401 (MCD‐PEPTIDE), A PEPTIDE FROM THE VENOM OF THE BEE Apis mellifera (L.)

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