Melittin

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title: "Melittin" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["antimicrobial-peptides", "insect-immunity", "insect-proteins"] topic_path: "general/antimicrobial-peptides" source: "https://en.wikipedia.org/wiki/Melittin" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::data[format=table title="Infobox protein family"]

FieldValue
SymbolMelittin
NameMelittin
imagePDB 2mlt EBI.jpg
captionMelittin
PfamPF01372
InterProIPR002116
SCOP2mlt
TCDB1.C.18
OPM family151
OPM protein2mlt
::

| Symbol = Melittin | Name = Melittin | image = PDB 2mlt EBI.jpg | width = | caption = Melittin | Pfam = PF01372 | Pfam_clan = | InterPro = IPR002116 | SMART = | PROSITE = | MEROPS = | SCOP = 2mlt | TCDB = 1.C.18 | OPM family = 151 | OPM protein = 2mlt | CAZy = | CDD = | Verifiedfields = changed | Watchedfields = changed | verifiedrevid = 414059490 | ImageFile= | ImageSize=275px | IUPACName= | OtherNames= | Reference= |Section1={{Chembox Identifiers | CASNo_Ref = | CASNo=20449-79-0 | ChEBI_Ref = | ChEBI = 6736 | ChEMBL_Ref = | ChEMBL = 412927 | UNII_Ref = | UNII = 24VT8NVE75 | PubChem = 16133648 | ChemSpiderID_Ref = | ChemSpiderID = 17290230 | SMILES = CCC(C)C(C(=O)NCC(=O)NC(C)C(=O)NC(C(C)C)C(=O)NC(CC(C)C)C(=O)NC(CCCCN)C(=O)NC(C(C)C)C(=O)NC(CC(C)C)C(=O)NC(C(C)O)C(=O)NC(C(C)O)C(=O)NCC(=O)NC(CC(C)C)C(=O)N1CCCC1C(=O)NC(C)C(=O)NC(CC(C)C)C(=O)NC(C(C)CC)C(=O)NC(CO)C(=O)NC(Cc2c[nH]c3c2cccc3)C(=O)NC(C(C)CC)C(=O)NC(CCCCN)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCCCN)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCC(=O)N)C(=O)NC(CCC(=O)N)C(=O)N)NC(=O)CN | InChI = 1/C131H229N39O31/c1-23-71(16)102(163-97(176)60-135)122(194)146-62-98(177)148-74(19)109(181)164-100(69(12)13)124(196)160-88(55-65(4)5)116(188)155-84(41-30-33-51-134)115(187)165-101(70(14)15)125(197)161-90(57-67(8)9)118(190)168-106(77(22)173)128(200)169-105(76(21)172)123(195)147-63-99(178)150-92(58-68(10)11)129(201)170-54-36-44-94(170)121(193)149-75(20)108(180)158-89(56-66(6)7)117(189)166-104(73(18)25-3)127(199)162-93(64-171)120(192)159-91(59-78-61-145-80-38-27-26-37-79(78)80)119(191)167-103(72(17)24-2)126(198)157-83(40-29-32-50-133)111(183)154-85(42-34-52-143-130(139)140)112(184)152-82(39-28-31-49-132)110(182)153-86(43-35-53-144-131(141)142)113(185)156-87(46-48-96(137)175)114(186)151-81(107(138)179)45-47-95(136)174/h26-27,37-38,61,65-77,81-94,100-106,145,171-173H,23-25,28-36,39-60,62-64,132-135H2,1-22H3,(H2,136,174)(H2,137,175)(H2,138,179)(H,146,194)(H,147,195)(H,148,177)(H,149,193)(H,150,178)(H,151,186)(H,152,184)(H,153,182)(H,154,183)(H,155,188)(H,156,185)(H,157,198)(H,158,180)(H,159,192)(H,160,196)(H,161,197)(H,162,199)(H,163,176)(H,164,181)(H,165,187)(H,166,189)(H,167,191)(H,168,190)(H,169,200)(H4,139,140,143)(H4,141,142,144)/t71-,72-,73-,74-,75-,76+,77+,81-,82-,83-,84-,85-,86-,87-,88-,89-,90-,91-,92-,93-,94-,100-,101-,102-,103-,104-,105-,106-/m0/s1 | InChIKey = VDXZNPDIRNWWCW-JFTDCZMZBB | StdInChI_Ref = | StdInChI = 1S/C131H229N39O31/c1-23-71(16)102(163-97(176)60-135)122(194)146-62-98(177)148-74(19)109(181)164-100(69(12)13)124(196)160-88(55-65(4)5)116(188)155-84(41-30-33-51-134)115(187)165-101(70(14)15)125(197)161-90(57-67(8)9)118(190)168-106(77(22)173)128(200)169-105(76(21)172)123(195)147-63-99(178)150-92(58-68(10)11)129(201)170-54-36-44-94(170)121(193)149-75(20)108(180)158-89(56-66(6)7)117(189)166-104(73(18)25-3)127(199)162-93(64-171)120(192)159-91(59-78-61-145-80-38-27-26-37-79(78)80)119(191)167-103(72(17)24-2)126(198)157-83(40-29-32-50-133)111(183)154-85(42-34-52-143-130(139)140)112(184)152-82(39-28-31-49-132)110(182)153-86(43-35-53-144-131(141)142)113(185)156-87(46-48-96(137)175)114(186)151-81(107(138)179)45-47-95(136)174/h26-27,37-38,61,65-77,81-94,100-106,145,171-173H,23-25,28-36,39-60,62-64,132-135H2,1-22H3,(H2,136,174)(H2,137,175)(H2,138,179)(H,146,194)(H,147,195)(H,148,177)(H,149,193)(H,150,178)(H,151,186)(H,152,184)(H,153,182)(H,154,183)(H,155,188)(H,156,185)(H,157,198)(H,158,180)(H,159,192)(H,160,196)(H,161,197)(H,162,199)(H,163,176)(H,164,181)(H,165,187)(H,166,189)(H,167,191)(H,168,190)(H,169,200)(H4,139,140,143)(H4,141,142,144)/t71-,72-,73-,74-,75-,76+,77+,81-,82-,83-,84-,85-,86-,87-,88-,89-,90-,91-,92-,93-,94-,100-,101-,102-,103-,104-,105-,106-/m0/s1 | StdInChIKey_Ref = | StdInChIKey = VDXZNPDIRNWWCW-JFTDCZMZSA-N | MeSHName=Melitten |Section2={{Chembox Properties | Formula=C131H229N39O31 | MolarMass=2846.46266 | Appearance= | Density= | MeltingPt= | BoilingPt= | Solubility= |Section3={{Chembox Hazards | MainHazards= | FlashPt= | AutoignitionPt =

Melittin is the main component (40–60% of the dry weight) and the major pain-producing substance of honeybee (Apis mellifera) venom. Melittin is a basic peptide consisting of 26 amino acids.

Function

The principal function of melittin as a component of bee venom is to cause pain and destruction of tissue of intruders that threaten a beehive. However, melittin is expressed, not only in the venom gland, but also in other tissues when the bee is infected with various pathogens. The over-expression of melittin (as well as secapin, another venom molecule) in infected honey bees may indicate that it plays a role in the immune response of bees to infectious diseases.

Structure

Melittin is a small peptide with no disulfide bridge; the N-terminal part of the molecule is predominantly hydrophobic and the C-terminal part is hydrophilic and strongly basic. In water, it forms a tetramer, but it also can spontaneously integrate itself into cell membranes.

Mechanism of action

Injection of melittin into animals and humans causes pain sensations. It has strong surface effects on cell membranes, causing pore formation in epithelial cells and the destruction of red blood cells. Melittin also activates nociceptor (pain receptor) cells through a variety of mechanisms.

Melittin can open thermal nociceptor TRPV1 channels via cyclooxygenase metabolites, resulting in depolarization of nociceptor cells. The pore-forming effects in cells cause the release of pro-inflammatory cytokines. It also activates G-protein-coupled receptor-mediated opening of transient receptor potential channels. Finally, melittin up-regulates the expression of Nav1.8 and Nav1.9 sodium channels in nociceptor cell, causing long-term action-potential firing and pain sensation.

Melittin inhibits protein kinase C, Ca2+/calmodulin-dependent protein kinase II, myosin light chain kinase, and Na+/K+-ATPase (synaptosomal membrane). Melittin blocks transport pumps such as the Na+-K+-ATPase and the H+-K+-ATPase.

Toxicity of a bee sting

Melittin is the main compound in bee venom, accounting for its potential lethality, caused by an anaphylactic reaction in some people. At the sites of multiple stings, localized pain, swelling, and skin redness occur, and if bees are swallowed, life-threatening swelling of the throat and respiratory passages may develop.

Use

Bee venom therapy has been used in traditional medicine for treating various disorders, although its non-specific toxicity has limited scientific research on its potential effects.

Gallery

File:"Melittin" from the series "The Building Blocks of Life".jpg|Steel sculpture based on the structure of melittin by Julian Voss-Andreae

References

References

  1. [https://pubchem.ncbi.nlm.nih.gov/compound/16129627 Melitten - Compound Summary], [[PubChem]].
  2. (2016). "Melittin, the Major Pain-Producing Substance of Bee Venom". Neuroscience Bulletin.
  3. (March 2017). "Unity in defence: honeybee workers exhibit conserved molecular responses to diverse pathogens". BMC Genomics.
  4. (1982). "The structure of melittin. II. Interpretation of the structure". The Journal of Biological Chemistry.
  5. (2 March 2024). "Bee venom". Drugs.com.
  6. (2017). "Melittin, a major peptide component of bee venom, and its conjugates in cancer therapy". Cancer Letters.
  7. (2016). "Application of bee venom and its main constituent melittin for cancer treatment". Cancer Chemotherapy and Pharmacology.

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antimicrobial-peptidesinsect-immunityinsect-proteins