HighlypuresyntheticMelittin
MelittinisamajorconstituentofthebeevenomofApismellifera.TheN-terminalpartofMelittin is hydrophobic andtheC-terminalpartis hydrophilic.Melittinaccumulatesincellmembranewhichleadstovariouseffects.Itcanbeusedtostudylipid-proteininteractionsinmembranes.Melittinhasdemonstratedinterestingpropertiesinpre-clinicalstudies asantimicrobialsubstance,asdrugagainstrheumatoidarthritis,arteriosclerosis,cancerorasdrugdeliverysystem.SmartoxBiotechnologyoffershighlypuresyntheticMelittin.
Description:
AAsequence: GIGAVLKVLTTGLPALISWIKRKRQQ-NH2
Length(aa):26
Formula:C131H229N39O31
MolecularWeight:2846,56Da
Appearance:whitelyophilizedsolid
Solubility:waterorsalinebuffer
CASnumber:20449-79-0
Source:synthetic
Purityrate:>95%
Reference:
ThreeValuablePeptidesfromBeeandWaspVenomsforTherapeuticandbiotechnologicalUse:Melittin,ApaminandMastoparan.
Whileknowledgeofthecompositionandmodeofactionofbeeandwaspvenomsdatesback50years,thetherapeuticvalueofthesetoxinsremainsrelativelyunexploded.Thepropertiesofthesevenomsarenowbeingstudiedwiththeaimtodesignanddevelopnewtherapeuticdrugs.Farfromevaluatingtheextensivenumberofmonographs,journalsandbooksrelatedtobeeandwaspvenomsandthetherapeuticeffectofthesetoxinsinnumerousdiseases,thefollowingreviewfocusesonthethreemostcharacterizedpeptides,namelymelittin,apamin,andmastoparan.Here,weupdateinformationrelatedtothesecompoundsfromtheperspectiveofappliedscienceanddiscusstheirpotentialtherapeuticandbiotechnologicalapplicationsinbiomedicine.
ConformationalStatesofMelittinataBilayerInterface.
Thedistributionofpeptideconformationsinthemembraneinterfaceiscentraltopartitioningenergetics.Molecular-dynamicssimulationsenablecharacterizationofin-membranestructuraldynamics.Here,wedescribemelittinpartitioningintodioleoylphosphatidylcholinelipidsusingCHARMMandOPLSforcefields.AlthoughtheOPLSsimulationfailedtoreproduceexperimentalresults,theCHARMMsimulationreportedwasconsistentwithexperiments.TheCHARMMsimulationshowedmelittintoberepresentedbyanarrowdistributionoffoldingstatesinthemembraneinterface.
Melittin:amembrane-activepeptidewithdiversefunctions
MelittinistheprincipaltoxiccomponentinthevenomoftheEuropeanhoneybeeApismelliferaandisacationic,hemolyticpeptide.Itisasmalllinearpeptidecomposedof26aminoacidresiduesinwhichtheamino-terminalregionispredominantlyhydrophobicwhereasthecarboxy-terminalregionishydrophilicduetothepresenceofastretchofpositivelychargedaminoacids.Thisamphiphilicpropertyofmelittinhasresultedinmelittinbeingusedasasuitablemodelpeptideformonitoringlipid-proteininteractionsinmembranes.Inthisreview,thesolutionandmembranepropertiesofmelittinarehighlighted,withanemphasisonmelittin-membraneinteractionusingbiophysicalapproaches.Therecentapplicationsofmelittininvariouscellularprocessesarediscussed.
Theactionsofmelittinonmembranes
DempseyCE(1990)Theactionsofmelittinonmembranes.BiochimBiophysActa. PubMedlink
Themolecularmechanismsunderlyingthevariouseffectsofmelittinonmembraneshavenotbeencompletelydefinedandmuchoftheevidencedescribedindicatesthatdifferentmolecularmechanismsmayunderliedifferentactionsofthepeptide.IdeasabouttheformationoftranSBIlayeraggregatesofmelittinundertheinfluenceofatransbilayerpotential,andforbilayerstructuralperturbationarisingfromthelocationofthepeptidehelixwithintheheadgroupregionofthemembranehavebeenmadebasedonthecrystalstructureofthepeptide,thekineticsandconcentrationdependenceofmelittinsmembraneactions,togetherwithsimpleideasabouttheconformationalpropertiesofamphipathichelicalpeptidesandtheirinteractionswithmembranes…
