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Amylin (8-37) (human)

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Amylin (8-37) (human), a fragment of human Amylin, readily forms fibrils in vitro and exhibits direct vasodilation effect in isolated rat mesenteric resistance arteries. Human amylin is a small hormone secreted by pancreatic beta cells, which forms aggregates in insulin-deficient metabolism and is a pathological feature of type II diabetes.

Category

Functional Peptides

Catalog number

BAT-015118

CAS number

135702-23-7

Molecular Formula

C138H216N42O45

Molecular Weight

3183.48

Specification
Reference Reading

IUPAC Name

(2S)-N-[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-4-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-4-amino-1-[[(2S)-4-amino-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S,3S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S,3R)-1-[[(2S)-4-amino-1-[[(2S)-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-methyl-1-oxobutan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-(1H-imidazol-4-yl)-1-oxopropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]-2-[[(2S,3R)-2-[[(2S)-2-aminopropanoyl]amino]-3-hydroxybutanoyl]amino]pentanediamide

Synonyms

H-Ala-Thr-Gln-Arg-Leu-Ala-Asn-Phe-Leu-Val-His-Ser-Ser-Asn-Asn-Phe-Gly-Ala-Ile-Leu-Ser-Ser-Thr-Asn-Val-Gly-Ser-Asn-Thr-Tyr-NH2; L-alanyl-L-threonyl-L-glutaminyl-L-arginyl-L-leucyl-L-alanyl-L-asparagyl-L-phenylalanyl-L-leucyl-L-valyl-L-histidyl-L-seryl-L-seryl-L-asparagyl-L-asparagyl-L-phenylalanyl-glycyl-L-alanyl-L-isoleucyl-L-leucyl-L-seryl-L-seryl-L-threonyl-L-asparagyl-L-valyl-glycyl-L-seryl-L-asparagyl-L-threonyl-L-tyrosinamide; Human IAPP (8-37)

Appearance

White Powder

Purity

≥95%

Density

1.51±0.1 g/cm3 (Predicted)

Sequence

ATQRLANFLVHSSNNFGAILSSTNVGSNTY-NH2

Storage

Store at -20°C

Solubility

Soluble in Acetonitrile, Water

InChI

InChI=1S/C138H216N42O45/c1-19-65(12)106(134(222)168-81(40-61(4)5)118(206)171-93(56-183)130(218)174-95(58-185)131(219)180-109(71(18)188)137(225)170-90(50-101(145)195)125(213)175-104(63(8)9)132(220)152-53-103(197)156-91(54-181)127(215)167-89(49-100(144)194)126(214)179-108(70(17)187)136(224)159-79(110(146)198)42-74-32-34-76(189)35-33-74)177-113(201)67(14)154-102(196)52-151-114(202)83(43-72-27-22-20-23-28-72)163-122(210)87(47-98(142)192)165-123(211)88(48-99(143)193)166-128(216)92(55-182)173-129(217)94(57-184)172-120(208)85(45-75-51-149-59-153-75)169-133(221)105(64(10)11)176-124(212)82(41-62(6)7)162-119(207)84(44-73-29-24-21-25-30-73)164-121(209)86(46-97(141)191)160-112(200)68(15)155-117(205)80(39-60(2)3)161-115(203)77(31-26-38-150-138(147)148)157-116(204)78(36-37-96(140)190)158-135(223)107(69(16)186)178-111(199)66(13)139/h20-25,27-30,32-35,51,59-71,77-95,104-109,181-189H,19,26,31,36-50,52-58,139H2,1-18H3,(H2,140,190)(H2,141,191)(H2,142,192)(H2,143,193)(H2,144,194)(H2,145,195)(H2,146,198)(H,149,153)(H,151,202)(H,152,220)(H,154,196)(H,155,205)(H,156,197)(H,157,204)(H,158,223)(H,159,224)(H,160,200)(H,161,203)(H,162,207)(H,163,210)(H,164,209)(H,165,211)(H,166,216)(H,167,215)(H,168,222)(H,169,221)(H,170,225)(H,171,206)(H,172,208)(H,173,217)(H,174,218)(H,175,213)(H,176,212)(H,177,201)(H,178,199)(H,179,214)(H,180,219)(H4,147,148,150)/t65-,66-,67-,68-,69+,70+,71+,77-,78-,79-,80-,81-,82-,83-,84-,85-,86-,87-,88-,89-,90-,91-,92-,93-,94-,95-,104-,105-,106-,107-,108-,109-/m0/s1

InChI Key

OBFZUAVBRVNJDZ-AWNVCVQVSA-N

Canonical SMILES

CCC(C)C(C(=O)NC(CC(C)C)C(=O)NC(CO)C(=O)NC(CO)C(=O)NC(C(C)O)C(=O)NC(CC(=O)N)C(=O)NC(C(C)C)C(=O)NCC(=O)NC(CO)C(=O)NC(CC(=O)N)C(=O)NC(C(C)O)C(=O)NC(CC1=CC=C(C=C1)O)C(=O)N)NC(=O)C(C)NC(=O)CNC(=O)C(CC2=CC=CC=C2)NC(=O)C(CC(=O)N)NC(=O)C(CC(=O)N)NC(=O)C(CO)NC(=O)C(CO)NC(=O)C(CC3=CNC=N3)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC4=CC=CC=C4)NC(=O)C(CC(=O)N)NC(=O)C(C)NC(=O)C(CC(C)C)NC(=O)C(CCCNC(=N)N)NC(=O)C(CCC(=O)N)NC(=O)C(C(C)O)NC(=O)C(C)N

1. Amylin or CGRP (8-37) fragments reverse amylin-induced inhibition of 14C-glycogen accumulation

R O Deems, F Cardinaux, R W Deacon, D A Young Biochem Biophys Res Commun. 1991 Nov 27;181(1):116-20. doi: 10.1016/s0006-291x(05)81389-0.

The peptides amylin and calcitonin-gene related peptide (CGRP) have been shown to have similar effects on glycogen metabolism in vivo and in vitro. However, it is not clear whether they act via separate receptors. Peptide fragments based on the amino acid sequence of amylin or CGRP were evaluated for their ability to inhibit the action of the peptides in vitro. Insulin-stimulated glycogen turnover, as measured by 14C-glycogen accumulation, was inhibited about 70% by amylin (10nM) and 85% by CGRP (10nM). In the absence of exogenous peptide, peptide fragments based on the 8-37 and 10-37 amino acid sequences of rat amylin (10 uM) had no affect on 14C-glycogen accumulation. In the presence of amylin (10nM), the 8-37 and 10-37 fragments blocked amylin-induced inhibition of 14C-glycogen accumulation 100% and 11.4%, respectively. The 8-37 and 10-37 amylin fragments blocked CGRP inhibition of 14C-glycogen accumulation by 23.2% or 28.6%, respectively. The CGRP 8-37 fragment was equally effective as the amylin 8-37 reversing the effects of amylin than at reversing the effects of CGRP. These results demonstrate that amylin (8-37) completely antagonizes the effects of amylin with limited ability to block CGRP. Removing the eighth and ninth amino acids reduced the effectiveness of the inhibitor by about 90%.

2. Reversal of the inhibitory effects of calcitonin gene-related peptide (CGRP) and amylin on insulin secretion by the 8-37 fragment of human CGRP

R A Silvestre, M Salas, P Dégano, E Peiró, J Marco Biochem Pharmacol. 1993 Jun 9;45(11):2343-7. doi: 10.1016/0006-2952(93)90209-f.

The 8-37 fragment of human calcitonin gene-related peptide [(8-37)hCGRP] antagonizes the effects of calcitonin gene-related peptide (CGRP) and amylin in a number of tissues. We have studied the influence of (8-37)hCGRP on the effects of both CGRP and amylin on insulin secretion. In the perfused rat pancreas, homologous CGRP and amylin, at 75 pM, exerted comparable inhibitory effects on the insulin response to 9 mM glucose (ca. 70%; P < 0.025). These effects were antagonized by (8-37)hCGRP (1 microM). Our results suggest that CGRP and amylin act on the B-cell, at least in part, through a common receptor.

3. Rat amylin-(8-37) enhances insulin action and alters lipid metabolism in normal and insulin-resistant rats

M Hettiarachchi, S Chalkley, S M Furler, Y S Choong, M Heller, G J Cooper, E W Kraegen Am J Physiol. 1997 Nov;273(5):E859-67. doi: 10.1152/ajpendo.1997.273.5.E859.

To clarify roles of amylin, we investigated metabolic responses to rat amylin-(8-37), a specific amylin antagonist, in normal and insulin-resistant, human growth hormone (hGH)-infused rats. Fasting conscious rats were infused with saline or hGH, each with and without amylin-(8-37) (0.125 mumol/h), over 5.75 h. At 3.75 h, a hyperinsulinemic (100 mU/l) clamp with bolus 2-deoxy-D-[3H]glucose and [14C]glucose was started. hGH infusion led to prompt (2- to 3-fold) basal hyperamylinemia (P < 0.02) and hyperinsulinemia. Amylin-(8-37) reduced plasma insulin (P < 0.001) and enhanced several measures of whole body and muscle insulin sensitivity (P < 0.05) in both saline- and hGH-infused rats. Amylin-(8-37) corrected hGH-induced liver insulin resistance, increased basal plasma triglycerides and lowered plasma nonesterified fatty acids in both groups, and reduced muscle triglyceride and total long-chain acyl-CoA content in saline-treated rats (P < 0.05). In isolated soleus muscle, amylin-(8-37) blocked amylin-induced inhibition of glycogen synthesis but had no effect in the absence of amylin. Thus 1) hyperamylinemia accompanies insulin resistance induced by hGH infusion; 2) amylin-(8-37) increases whole body and muscle insulin sensitivity and consistently reduces basal insulin levels in normal and hGH-induced insulin resistant rats; and 3) amylin-(8-37) elicits a significant alteration of in vivo lipid metabolism. These findings support a role of amylin in modulating insulin action and suggest that this could be mediated by effects on lipid metabolism.