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ACTH 22-39

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ACTH (22-39) is a peptide fragment of ACTH, a tropic hormone produced by the anterior pituitary.

Category

Peptide Inhibitors

Catalog number

BAT-006109

CAS number

37548-29-1

Molecular Formula

C90H125N19O32

Molecular Weight

1985.06

Size	Price	Stock	Quantity
2.5 mg	$239	In stock
5 mg	$419	In stock

Specification
Reference Reading

IUPAC Name

(4S)-4-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-4-amino-2-[[(2S)-1-[(2S)-2-[[(2S)-2-amino-3-methylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]pyrrolidine-2-carbonyl]amino]-4-oxobutanoyl]amino]acetyl]amino]propanoyl]amino]-4-carboxybutanoyl]amino]-3-carboxypropanoyl]amino]-4-carboxybutanoyl]amino]-3-hydroxypropanoyl]amino]propanoyl]amino]-5-[[(2S)-1-[[(2S)-1-[(2S)-2-[[(2S)-1-[[(2S)-4-carboxy-1-[[(1S)-1-carboxy-2-phenylethyl]amino]-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxo-3-phenylpropan-2-yl]amino]-1-oxopropan-2-yl]amino]-5-oxopentanoic acid

Synonyms

Adrenocorticoptropic Hormone Fragment 22-39; ACTH (22-39) (human); H-Val-Tyr-Pro-Asn-Gly-Ala-Glu-Asp-Glu-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-OH; L-valyl-L-tyrosyl-L-prolyl-L-asparagyl-glycyl-L-alanyl-L-alpha-glutamyl-L-alpha-aspartyl-L-alpha-glutamyl-L-seryl-L-alanyl-L-alpha-glutamyl-L-alanyl-L-phenylalanyl-L-prolyl-L-leucyl-L-alpha-glutamyl-L-phenylalanine; beta-Cell-Tropin

Appearance

Solid

Purity

≥95% by HPLC

Density

1.386±0.06 g/cm3 (Predicted)

Boiling Point

2252.3±65.0°C (Predicted)

Sequence

VYPNGAEDESAEAFPLEF

Storage

Store at -20°C

Solubility

Soluble in Water

InChI

InChI=1S/C90H125N19O32/c1-44(2)36-57(82(132)99-55(28-32-70(118)119)80(130)106-62(90(140)141)39-50-18-12-9-13-19-50)102-85(135)64-20-14-34-108(64)88(138)60(37-49-16-10-8-11-17-49)104-76(126)48(7)95-78(128)53(26-30-68(114)115)97-75(125)47(6)96-84(134)63(43-110)107-81(131)56(29-33-71(120)121)100-83(133)59(41-72(122)123)101-79(129)54(27-31-69(116)117)98-74(124)46(5)94-67(113)42-93-77(127)58(40-66(91)112)103-86(136)65-21-15-35-109(65)89(139)61(105-87(137)73(92)45(3)4)38-51-22-24-52(111)25-23-51/h8-13,16-19,22-25,44-48,53-65,73,110-111H,14-15,20-21,26-43,92H2,1-7H3,(H2,91,112)(H,93,127)(H,94,113)(H,95,128)(H,96,134)(H,97,125)(H,98,124)(H,99,132)(H,100,133)(H,101,129)(H,102,135)(H,103,136)(H,104,126)(H,105,137)(H,106,130)(H,107,131)(H,114,115)(H,116,117)(H,118,119)(H,120,121)(H,122,123)(H,140,141)/t46-,47-,48-,53-,54-,55-,56-,57-,58-,59-,60-,61-,62-,63-,64-,65-,73-/m0/s1

InChI Key

VNYTZTMGIJDKGF-SYGRCPSDSA-N

Canonical SMILES

CC(C)CC(C(=O)NC(CCC(=O)O)C(=O)NC(CC1=CC=CC=C1)C(=O)O)NC(=O)C2CCCN2C(=O)C(CC3=CC=CC=C3)NC(=O)C(C)NC(=O)C(CCC(=O)O)NC(=O)C(C)NC(=O)C(CO)NC(=O)C(CCC(=O)O)NC(=O)C(CC(=O)O)NC(=O)C(CCC(=O)O)NC(=O)C(C)NC(=O)CNC(=O)C(CC(=O)N)NC(=O)C4CCCN4C(=O)C(CC5=CC=C(C=C5)O)NC(=O)C(C(C)C)N

1. Beta-cell tropin: synthesis and biological activity

G W Taylor, A Beloff-Chain, S J Dunmore, E F Nurse, J Humphries, H R Morris Biochem Biophys Res Commun . 1983 Jul 29;114(2):763-6. doi: 10.1016/0006-291x(83)90846-x.

The structure of beta-cell tropin, an insulin secretagogue released by the neuro-intermediate lobe of the obese (ob/ob) mouse, has recently been determined as the 22-39 moiety of ACTH. A method for the preparation of this octadecapeptide using mild solid-phase procedures followed by preparative high pressure liquid chromatography is described. The molecular weight of the synthetic peptide has been confirmed by Fast Atom Bombardment mass spectrometry. Synthetic beta-cell tropin is indistinguishable in its chromatographic, antigenic and biological properties from natural beta-cell tropin.

2. Beta-cell tropin- and glucose-induced hypersecretion of insulin and amylin from perfused fatty rat pancreas

A Beloff-Chain, S J Dunmore, D C Hislop, J L Morton, M A Cawthorne J Endocrinol . 1993 Jun;137(3):375-81. doi: 10.1677/joe.0.1370375.

The neurointermediate pituitary peptide beta-cell tropin (BCT) has potent insulin-releasing and lipogenic properties and is elevated in obesity and type-2 diabetes. The effects of BCT and glucose on the release of insulin and amylin from the perfused pancreas of obese 'fatty' (fa/fa) rats and lean (Fa/?) controls were measured. Pancreata were perfused, sequentially, with buffer containing: 5.6 mmol glucose/l (basal); basal glucose +/- 0.5 nmol BCT/l; 16.7 mmol glucose/l (high). Insulin and amylin release during basal glucose treatment was eight to nine times greater from pancreata from fatty than from lean rats. BCT induced a fivefold greater monophasic insulin and amylin release from fatty compared with lean pancreata. When not preceded by BCT there was a twofold greater high glucose-induced amylin release from fatty pancreata but no difference in insulin secretion. When preceded by BCT stimulation, high glucose induced twofold greater insulin and fourfold larger amylin release from fatty compared with lean pancreata. Molar secretion ratios of insulin:amylin varied between 30:1 and 50:1. In view of the elevated levels of BCT found in the fatty rat and in the light of the above findings, it is concluded that the peptide may have a role in the development of hyperinsulinaemia, hyperamylinaemia and insulin resistance in this animal model of obesity and diabetes.

3. The effects of structural modifications on the insulin-releasing activity of beta-cell-tropin

M Panico, A Beloff-Chain, S J Dunmore, A T Etienne, H R Morris Biochem J . 1987 Jun 15;244(3):797-800. doi: 10.1042/bj2440797.

The minimal effective concentration of the pituitary insulin secretagogue beta-cell-tropin (beta-CT) on the in vitro perfused pancreas was established and the effects of various modifications of the peptide on its potency were tested: iodination with 127I and acetylation reduced the insulin-releasing activity of beta-cell-tropin, and the C-terminal fragments beta-CT-(2-18), beta-CT-(3-18) and beta-CT-(6-18) were all less potent than the intact molecule; beta-CT-(1-6) was not active and did not inhibit beta-CT-induced insulin release.