For research use only. Not for therapeutic Use.
Melittin（Cat No.:R034622）, is a naturally occurring peptide found in bee venom, primarily from honeybees (Apis mellifera). It is one of the major components of bee venom, known for its potent biological effects. Melittin is a small, linear peptide consisting of 26 amino acid residues. Its main biological activity is its ability to disrupt cell membranes, leading to cell lysis and cytotoxicity. Research has shown that melittin possesses antimicrobial, anti-inflammatory, and anticancer properties. It is also being studied for potential therapeutic applications, such as drug delivery systems and as a treatment for certain diseases.
| Catalog Number | R034622 |
| CAS Number | 20449-79-0 |
| Synonyms | Melittin (major); Melittin (honeybee); 16: PN: WO2010149795 SEQID: 53 claimed protein; 72: PN: US7381704 SEQID: 72 claimed sequence; Bee Venom Melittin; Forapin; Forapine; Honeybee Melittin; Melittin (Apis cerana); Melittin I; |
| Molecular Formula | C131H229N39O31 |
| Purity | ≥95% |
| Target | Phospholipase |
| Storage | -20°C |
| IUPAC Name | (2S)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[2-[[(2S,3R)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S,3S)-2-[(2-aminoacetyl)amino]-3-methylpentanoyl]amino]acetyl]amino]propanoyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxybutanoyl]amino]acetyl]amino]-4-methylpentanoyl]pyrrolidine-2-carbonyl]amino]propanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-3-methylpentanoyl]amino]hexanoyl]amino]-5-carbamimidamidopentanoyl]amino]hexanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-oxopentanoyl]amino]pentanediamide |
| 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 |
| InChIKey | VDXZNPDIRNWWCW-JFTDCZMZSA-N |
| 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(CC2=CNC3=CC=CC=C32)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 |
| Reference | – Raynor et al., /Membrane interactions of amphiphilic polypeptides mastoparan, melittin, polymyxin B, and cardiotoxin./ <I>J. Biol. Chem.</I> 1991 266(5):2753-2758<br /><br />- Schweitz, /Lethal potency in mice of toxins from scorpion, sea anemone, snake and bee venoms following intraperitoneal and intracisternal injection./ Toxicon (1984). 22:308-311<br /><br />- Habermann, /Bee and wasp venoms: the biochemistry and pharmacology of their peptides and enzymes are reviewed./ Science (1972). 177:314-322<br /><br /><br /><br /> |
