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AC 187
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AC 187 is a potent amylin receptor antagonist (IC50 = 0.48 nM) displayiing 38- and 400-fold selectivity over calcitonin and CGRP receptors respectively. It inhibits amyloid β-induced neurotoxicity by attenuating the activation of initiator and effector caspases in vitro. It increases glucagon secretion, accelerates gastric emptying, alters plasma glucose levels and increases food intake in vivo.

Peptide Inhibitors
Catalog number
CAS number
Molecular Formula
Molecular Weight
AC 187
(4S)-4-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-acetamido-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]acetyl]amino]-6-aminohexanoyl]amino]-4-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-[[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-5-amino-1-[[(2S,3R)-1-[[(2S)-1-[(2S)-2-[[(2S)-1-[[(2S,3R)-1-[[(2S)-4-amino-1-[[(2S,3R)-1-[[2-[[(2S)-1-[[(2S)-4-amino-1-[[(2S,3R)-1-[[(2S)-1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]carbamoyl]pyrrolidin-1-yl]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-(1H-imidazol-4-yl)-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-oxopentanoic acid
Ac-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Thr-Gly-Ser-Asn-Thr-Tyr-NH2; N-acetyl-L-valyl-L-leucyl-glycyl-L-lysyl-L-leucyl-L-seryl-L-glutaminyl-L-alpha-glutamyl-L-leucyl-L-histidyl-L-lysyl-L-leucyl-L-glutaminyl-L-threonyl-L-tyrosyl-L-prolyl-L-arginyl-L-threonyl-L-asparagyl-L-threonyl-glycyl-L-seryl-L-asparagyl-L-threonyl-L-tyrosinamide; AC187; salmon calcitonin (8-32) reduced; acetyl-(Asn30,Tyr32)sCT(8-37); AC-187
White Lyophilized Solid
1.49±0.1 g/cm3 (Predicted)
VLGKLSQELHKLQTYPRTNTGSNTY (Modifications: Val-1 = N-terminal Ac, Tyr-25 = C-terminal amide)
Store at -20°C
Soluble in Water
InChI Key
Canonical SMILES
1.Lactate production from the rat hindlimb is increased after glucose administration and is suppressed by a selective amylin antagonist: evidence for action of endogenous amylin in skeletal muscle.
Vine W;Smith P;LaChappell R;Rink TJ;Young AA Biochem Biophys Res Commun. 1995 Nov 13;216(2):554-9.
By serially measuring blood flow and venous-arterial lactate differences across the hindlimb of the fasted anesthetized rat, we examined (1) whether exogenous amylin increased muscle lactate production in vivo, (2) whether glucose administration increased muscle lactate production, and (3), by using the selective amylin antagonist AC187 to block endogenous peptide, whether amylin secreted in response to glucose could mediate muscle lactate production. Abdominal aortic flow was unchanged by any treatment. Hindlimb lactate production was increased by both 100 micrograms s.c. amylin (4.0 +/- 0.4 cf 2.6 +/- 0.3 mumol/min after saline, P < 0.05) and by infusion of 2mmol D-glucose (3.0 +/- 0.2 cf 2.3 +/- 0.2 mumole/hr after saline, P < 0.03). The increase in hindlimb lactate production was prevented by infusion of AC187 (mean post-treatment venoarterial delta-lactate 140 +/- 11 microM; n.s. vs saline-treated delta-lactate 154 +/- 10 microM; P < 0.05 vs glucose-treated delta-lactate 201 +/- 14 microM). These findings are consistent with endogenous amylin secreted in response to a glucose challenge having acted at skeletal muscle to release lactate.
2.Amylin stimulates proximal tubular sodium transport and cell proliferation in the rat kidney.
Harris PJ;Cooper ME;Hiranyachattada S;Berka JL;Kelly DJ;Nobes M;Wookey PJ Am J Physiol. 1997 Jan;272(1 Pt 2):F13-21.
In autoradiographic studies in anesthetized rats, 125I-labeled amylin binding was associated with proximal convoluted tubules but not distal tubules, interstitium, or glomeruli in the renal cortex. Split-drop micropuncture experiments showed that perfusion of the peritubular capillaries with amylin (10(-9) M) stimulated proximal tubular fluid absorption by 28%. This effect was inhibited by luminal addition of ethylisopropylamiloride, indicating mediation by a brush-border Na+/H+ exchanger. Intravenous infusion of an amylin binding antagonist, AC-187, reduced proximal fluid reabsorption (22%) in anesthetized rats, indicating a role for endogenous amylin in salt homeostasis. In primary cultures of rat proximal tubule cells, amylin (10(-7) M) stimulated proliferation with a potency equal to epidermal growth factor. Peptide antagonists (AC-187, AC-413, and AC-512) of the amylin binding sites in the renal cortex blocked the mitogenic action of amylin. We conclude that amylin acts on renal proximal tubules to promote sodium and water reabsorption and cell proliferation. These novel actions may have implications for the development of hypertension for example in non-insulin-dependent diabetes mellitus and obesity in which hyperamylinemia has been observed.
3.Studies of synthetic peptides of human apolipoprotein A-I containing tandem amphipathic alpha-helixes.
Mishra VK;Palgunachari MN;Datta G;Phillips MC;Lund-Katz S;Adeyeye SO;Segrest JP;Anantharamaiah GM Biochemistry. 1998 Jul 14;37(28):10313-24.
In mature human apolipoprotein A-I (apo A-I), the amino acid residues 1-43 are encoded by exon 3, whereas residues 44-243 are encoded by exon 4 of the apo A-I gene. The region encoded by exon 4 of the apo A-I gene contains 10 tandem amphipathic alpha-helixes; their location and the class to which they belong are as follows: helix 1 (44-65, class A1), helix 2 (66-87, class A1), helix 3 (88-98, class Y), helix 4 (99-120, class Y), helix 5 (121-142, class A1), helix 6 (143-164, class A1), helix 7 (165-186, class A1), helix 8 (187-208, class A1), helix 9 (209-219, class Y), and helix 10 (220-241, class Y). To examine the effects of multiple tandem amphipathic helixes compared to individual helixes of apo A-I on lipid association, we have studied lipid-associating properties of the following peptides: Ac-44-87-NH2 (peptide 1-2), Ac-66-98-NH2 (peptide 2-3), Ac-66-120-NH2 (peptide 2-3-4), Ac-88-120-NH2 (peptide 3-4), Ac-99-142-NH2 (peptide 4-5), Ac-121-164-NH2 (peptide 5-6), Ac-143-186-NH2 (peptide 6-7), Ac-165-208-NH2 (peptide 7-8), Ac-187-219-NH2 (peptide 8-9), and Ac-209-241-NH2 (peptide 9-10). To study lipid-associating properties of the region encoded by exon 3 of the apo A-I gene, 1-33-NH2 (peptide G) has also been studied.

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