مليتين melittin

مليتين^[1]
المُعرِّفات
رقم CAS
3D model (JSmol)	Interactive image;
ChEBI	CHEBI:6736 ;
ChEMBL	ChEMBL412927 ;
ChemSpider	17290230 ;
عناوين مواضيع طبية MeSH	{{{value}}}
PubChem CID	16133648;
UNII	24VT8NVE75 ;
	InChI InChI=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 Key: VDXZNPDIRNWWCW-JFTDCZMZSA-N ; 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 Key: VDXZNPDIRNWWCW-JFTDCZMZBB;
	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;
الخصائص
الصيغة الجزيئية	C131H229N39O31
كتلة مولية	2846.46266
	ما لم يُذكر غير ذلك، البيانات المعطاة للمواد في حالاتهم العيارية (عند 25 °س [77 °ف]، 100 kPa).
	verify (what is ?)
	مراجع الجدول

بنى الپروتين المتاحة:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Melittin
Melittin
	Melittin
المعرفات
الرمز	Melittin
Pfam	PF01372
InterPro	IPR002116
SCOP	2mlt
SUPERFAMILY	2mlt
TCDB	1.C.18
OPM superfamily	151
OPM protein	2mlt
Pfam
بنى الپروتين المتاحة:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

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.^[2]

الوظيفة

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.^{[بحاجة لمصدر]} However, melittin is expressed, not only in the venom gland, but also in other tissues when the bee is infected with various pathogens.^{[بحاجة لمصدر]} The over-expression of melittin (and also of 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.^[3]

البنية

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.^[4]

آلية العمل

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.^[2]

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.^[2]

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.^[2]

سمية لدغة النحل

Melittin is the main compound in bee venom, accounting for its potential lethality, caused by an anaphylactic reaction in some people.^[5] 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.^[5]

استخدام

Bee venom therapy has been used in traditional medicine for treating various disorders,^[6] although its non-specific toxicity has limited scientific research on its potential effects.^[7]

معرض

Steel sculpture based on the structure of melittin by Julian Voss-Andreae

المراجع

^ Melitten - Compound Summary, PubChem.
^ ^أ ^ب ^ت ^ث Chen J, Guan SM, Sun W, Fu H (2016). "Melittin, the Major Pain-Producing Substance of Bee Venom". Neuroscience Bulletin. 32 (3): 265–272. doi:10.1007/s12264-016-0024-y. PMC 5563768. PMID 26983715.
^ Doublet V, Poeschl Y, Gogol-Döring A, et al. (March 2017). "Unity in defence: honeybee workers exhibit conserved molecular responses to diverse pathogens". BMC Genomics. 18 (1): 207. doi:10.1186/s12864-017-3597-6. PMC 5333379. PMID 28249569.
^ Terwilliger TC, Eisenberg D (1982). "The structure of melittin. II. Interpretation of the structure" (PDF). The Journal of Biological Chemistry. 257 (11): 6016–6022. doi:10.1016/S0021-9258(20)65098-0. PMID 7076662.
^ ^أ ^ب "Bee venom". Drugs.com. 2 March 2024. Retrieved 15 July 2024.
^ Rady I, Siddiqui IA, Rady M, Mukhtar H (2017). "Melittin, a major peptide component of bee venom, and its conjugates in cancer therapy". Cancer Letters. 402: 16–31. doi:10.1016/j.canlet.2017.05.010. PMC 5682937. PMID 28536009.
^ Liu CC, Hao DJ, Zhang Q, An J, Zhao JJ, Chen B, Zhang LL, Yang H (2016). "Application of bee venom and its main constituent melittin for cancer treatment". Cancer Chemotherapy and Pharmacology. 78 (6): 1113–1130. doi:10.1007/s00280-016-3160-1. PMID 27677623. S2CID 12596298.

وصلات خارجية

MeSH Melitten

قالب:Membrane proteins قالب:Pore-forming toxins

?

[1] Melitten - Compound Summary, PubChem.

[Chen_2016-2] أ ^ب ^ت ^ث Chen J, Guan SM, Sun W, Fu H (2016). "Melittin, the Major Pain-Producing Substance of Bee Venom". Neuroscience Bulletin. 32 (3): 265–272. doi:10.1007/s12264-016-0024-y. PMC 5563768. PMID 26983715.

[3] Doublet V, Poeschl Y, Gogol-Döring A, et al. (March 2017). "Unity in defence: honeybee workers exhibit conserved molecular responses to diverse pathogens". BMC Genomics. 18 (1): 207. doi:10.1186/s12864-017-3597-6. PMC 5333379. PMID 28249569.

[Terwilliger_1982-4] Terwilliger TC, Eisenberg D (1982). "The structure of melittin. II. Interpretation of the structure" (PDF). The Journal of Biological Chemistry. 257 (11): 6016–6022. doi:10.1016/S0021-9258(20)65098-0. PMID 7076662.

[drugs-5] أ ^ب "Bee venom". Drugs.com. 2 March 2024. Retrieved 15 July 2024.

[Rady_2917-6] Rady I, Siddiqui IA, Rady M, Mukhtar H (2017). "Melittin, a major peptide component of bee venom, and its conjugates in cancer therapy". Cancer Letters. 402: 16–31. doi:10.1016/j.canlet.2017.05.010. PMC 5682937. PMID 28536009.

[Liu_2016-7] Liu CC, Hao DJ, Zhang Q, An J, Zhao JJ, Chen B, Zhang LL, Yang H (2016). "Application of bee venom and its main constituent melittin for cancer treatment". Cancer Chemotherapy and Pharmacology. 78 (6): 1113–1130. doi:10.1007/s00280-016-3160-1. PMID 27677623. S2CID 12596298.

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