Melanotan (MT)-II

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Melanotan (MT)-II
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Melanotan II is a potent full agonist of melanocortin-3 and melanocortin-4 receptors (Ki= 6.6, 34 for MC4, MC3 receptors respectively). Melanotan II stimulates erectile activity, and inhibits food intake and displays neuroprotective properties in vivo.

Category
Peptide Inhibitors
Catalog number
BAT-006134
CAS number
121062-08-6
Molecular Formula
C50H69N15O9
Molecular Weight
1024.18
Melanotan (MT)-II
Size Price Stock Quantity
10 mg $199 In stock
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IUPAC Name
(3S,6S,9R,12S,15S,23S)-15-[[(2S)-2-acetamidohexanoyl]amino]-9-benzyl-6-[3-(diaminomethylideneamino)propyl]-12-(1H-imidazol-5-ylmethyl)-3-(1H-indol-3-ylmethyl)-2,5,8,11,14,17-hexaoxo-1,4,7,10,13,18-hexazacyclotricosane-23-carboxamide
Synonyms
Melanotan II; MTII, Bremelanotide amide; Melanotan-II; MelanotanII; Ac-[Nle4Asp5D-Phe7Lys10]α-MSH-(4-10)-NH2; Ac-Nle-Asp-His-d-Phe-Arg-Trp-Lys-NH2, (2→7)-lactam
Appearance
White Lyophilized Powder
Purity
98%
Density
1.4±0.1 g/cm3
Sequence
XDHFRWK (Modifications: X = Nle & N-terminal Ac, Asp-2 = beta-Asp, Phe-4 = D-Phe, Lys-7 = epsilon-Lys, Cyclized = Asp-2-Lys-7, C-terminal amide)
Storage
Store at -20°C
Solubility
Soluble in Water (0.70 mg/mL)
InChI
InChI=1S/C50H69N15O9/c1-3-4-16-36(59-29(2)66)44(69)65-41-25-42(67)55-20-11-10-18-35(43(51)68)60-47(72)39(23-31-26-57-34-17-9-8-15-33(31)34)63-45(70)37(19-12-21-56-50(52)53)61-46(71)38(22-30-13-6-5-7-14-30)62-48(73)40(64-49(41)74)24-32-27-54-28-58-32/h5-9,13-15,17,26-28,35-41,57H,3-4,10-12,16,18-25H2,1-2H3,(H2,51,68)(H,54,58)(H,55,67)(H,59,66)(H,60,72)(H,61,71)(H,62,73)(H,63,70)(H,64,74)(H,65,69)(H4,52,53,56)/t35-,36-,37-,38+,39-,40-,41-/m0/s1
InChI Key
JDKLPDJLXHXHNV-MFVUMRCOSA-N
Canonical SMILES
CCCCC(C(=O)NC1CC(=O)NCCCCC(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC1=O)CC2=CN=CN2)CC3=CC=CC=C3)CCCN=C(N)N)CC4=CNC5=CC=CC=C54)C(=O)N)NC(=O)C
1.Characterization of Agouti-related protein binding to melanocortin receptors.
Yang YK;Thompson DA;Dickinson CJ;Wilken J;Barsh GS;Kent SB;Gantz I Mol Endocrinol. 1999 Jan;13(1):148-55.
Agouti-related protein (AGRP) is a naturally occurring antagonist of melanocortin action that is thought to play an important role in the hypothalamic control of feeding behavior. The exact mechanism of AGRP and Agouti protein action has been difficult to examine, in part because of difficulties in producing homogeneous forms of these molecules that can be used for direct binding assays. In this report we describe the application of chemical protein synthesis to the construction of two novel AGRP variants. Examination of the biological activity of the AGRP variants demonstrates that a truncated variant, human AGRP(87-132), a 46-amino acid variant based on the carboxyl-terminal cysteine-rich domain of AGRP, is equipotent to an 111-amino acid variant, mouse [Leu127Pro]AGRP (mature AGRP minus its signal sequence), in its ability to dose dependently inhibit alpha-MSH-generated cAMP generation at the cloned melanocortin receptors. Furthermore, deletion of the amino-terminal portion of the full-length variant did not alter the MCR subtype specificity of AGRP(87-132). Finally, iodination of human AGRP(87-132) provided a useful reagent with which the binding properties of AGRP could be analyzed.
2.Molecular determinants of ligand binding to the human melanocortin-4 receptor.
Yang YK;Fong TM;Dickinson CJ;Mao C;Li JY;Tota MR;Mosley R;Van Der Ploeg LH;Gantz I Biochemistry. 2000 Dec 5;39(48):14900-11.
To elucidate the molecular basis for the interaction of ligands with the human melanocortin-4 receptor (hMC4R), agonist structure-activity studies and receptor point mutagenesis were performed. Structure-activity studies of [Nle(4), D-Phe(7)]-alpha-melanocyte stimulating hormone (NDP-MSH) identified D-Phe7-Arg8-Trp9 as the minimal NDP-MSH fragment that possesses full agonist efficacy at the hMC4R. In an effort to identify receptor residues that might interact with amino acids in this tripeptide sequence 24 hMC4R transmembrane (TM) residues were mutated (the rationale for choosing specific receptor residues for mutation is outlined in the Results section). Mutation of TM3 residues D122 and D126 and TM6 residues F261 and H264 decreased the binding affinity of NDP-MSH 5-fold or greater, thereby identifying these receptor residues as sites potentially involved in the sought after ligand-receptor interactions. By examination of the binding affinities and potencies of substituted NDP-MSH peptides at receptor mutants, evidence was found that core melanocortin peptide residue Arg8 interacts at a molecular level with hMC4R TM3 residue D122. TM3 mutations were also observed to decrease the binding of hMC4R antagonists.
3.Bradykinin-induced phosphoinositide hydrolysis and Ca2+ mobilization in canine cultured tracheal epithelial cells.
Luo SF;Pan SL;Wu WB;Wang CC;Chiu CT;Tsai YJ;Yang CM Br J Pharmacol. 1999 Mar;126(6):1341-50.
1. Experiments were designed to differentiate the mechanisms and subtype of kinin receptors mediating the changes in intracellular Ca2+ concentration ([Ca2+]i) induced by bradykinin (BK) in canine cultured tracheal epithelial cells (TECs). 2. BK and Lys-BK caused an initial transient peak of [Ca2+]i in a concentration-dependent manner, with half-maximal stimulation (pEC50) obtained at 7.70 and 7.23, respectively. 3. Kinin B2 antagonists Hoe 140 (10 nM) and [D-Arg0, Hyp3, Thi5,8, D-Phe7]-BK (1 microM) had high affinity in antagonizing BK-induced Ca2+ response with pKB values of 8.90 and 6.99, respectively. 4. Pretreatment of TECs with pertussis toxin (100 ng ml(-1)) or cholera toxin (10 microg ml(-1)) for 24 h did not affect the BK-induced IP accumulation and [Ca2+]i changes in TECs. 5. Removal of Ca2+ by the addition of EGTA or application of Ca2+-channel blockers, verapamil, diltiazem, and Ni2+, inhibited the BK-induced IP accumulation and Ca2+ mobilization, indicating that Ca2+ influx was required for the BK-induced responses. 6. Addition of thapsigargin (TG), which is known to deplete intracellular Ca2+ stores, transiently increased [Ca2+]i in Ca2+-free buffer and subsequently induced Ca2+ influx when Ca2+ was re-added to this buffer.

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