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(Gln22)-Amyloid β-Protein (1-42)

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

(Gln22)-Amyloid β-Protein (1-42), the Dutch mutation (E22Q), aggregates more easily than the wild-type. The resulting fibrils show increased neurotoxicity.

Category

Functional Peptides

Catalog number

BAT-014555

CAS number

147335-12-4

Molecular Formula

C203H312N56O59S

Molecular Weight

4513.12

Specification
Reference Reading

IUPAC Name

(4S)-5-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-5-amino-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-5-amino-1-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-4-amino-1-[[(2S)-6-amino-1-[[2-[[(2S)-1-[[(2S,3S)-1-[[(2S,3S)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[2-[[2-[[(2S)-1-[[(2S)-1-[[(2S,3S)-1-[[(1S)-1-carboxyethyl]amino]-3-methyl-1-oxopentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-2-oxoethyl]amino]-2-oxoethyl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-3-methyl-1-oxopentan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-1-oxohexan-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]-3-carboxy-1-oxopropan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-3-(1H-imidazol-5-yl)-1-oxopropan-2-yl]amino]-3-(1H-imidazol-5-yl)-1-oxopropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-3-(1H-imidazol-5-yl)-1-oxopropan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-4-[[(2S)-2-[[(2S)-2-amino-3-carboxypropanoyl]amino]propanoyl]amino]-5-oxopentanoic acid

Synonyms

Amyloid β-Protein (1-42) Dutch Mutation; H-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Gln-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala-OH; L-alpha-aspartyl-L-alanyl-L-alpha-glutamyl-L-phenylalanyl-L-arginyl-L-histidyl-L-alpha-aspartyl-L-seryl-glycyl-L-tyrosyl-L-alpha-glutamyl-L-valyl-L-histidyl-L-histidyl-L-glutaminyl-L-lysyl-L-leucyl-L-valyl-L-phenylalanyl-L-phenylalanyl-L-alanyl-L-glutaminyl-L-alpha-aspartyl-L-valyl-glycyl-L-seryl-L-asparagyl-L-lysyl-glycyl-L-alanyl-L-isoleucyl-L-isoleucyl-glycyl-L-leucyl-L-methionyl-L-valyl-glycyl-glycyl-L-valyl-L-valyl-L-isoleucyl-L-alanine

Appearance

White Powder

Purity

≥90%

Sequence

DAEFRHDSGYEVHHQKLVFFAQDVGSNKGAIIGLMVGGVVIA

Storage

Store at -20°C

Solubility

Soluble in Acetonitrile, Water

InChI

InChI=1S/C203H312N56O59S/c1-28-106(20)164(195(310)221-91-150(269)229-130(71-98(4)5)181(296)239-129(66-70-319-27)179(294)252-158(100(8)9)193(308)219-87-147(266)216-88-152(271)251-160(102(12)13)198(313)256-163(105(18)19)199(314)259-165(107(21)29-2)200(315)228-112(26)202(317)318)258-201(316)166(108(22)30-3)257-169(284)109(23)225-148(267)89-217-171(286)122(51-40-42-67-204)234-188(303)139(81-146(209)265)245-192(307)143(94-261)231-151(270)92-220-194(309)159(101(10)11)253-191(306)141(83-157(280)281)246-176(291)125(58-62-144(207)263)232-168(283)111(25)227-180(295)133(73-113-45-34-31-35-46-113)242-184(299)135(75-115-49-38-33-39-50-115)248-196(311)162(104(16)17)255-190(305)131(72-99(6)7)240-173(288)123(52-41-43-68-205)235-175(290)126(59-63-145(208)264)237-185(300)136(77-117-84-212-95-222-117)244-187(302)138(79-119-86-214-97-224-119)249-197(312)161(103(14)15)254-178(293)128(61-65-154(274)275)238-182(297)132(76-116-54-56-120(262)57-55-116)230-149(268)90-218-172(287)142(93-260)250-189(304)140(82-156(278)279)247-186(301)137(78-118-85-213-96-223-118)243-174(289)124(53-44-69-215-203(210)211)236-183(298)134(74-114-47-36-32-37-48-114)241-177(292)127(60-64-153(272)273)233-167(282)110(24)226-170(285)121(206)80-155(276)277/h31-39,45-50,54-57,84-86,95-112,121-143,158-166,260-262H,28-30,40-44,51-53,58-83,87-94,204-206H2,1-27H3,(H2,207,263)(H2,208,264)(H2,209,265)(H,212,222)(H,213,223)(H,214,224)(H,216,266)(H,217,286)(H,218,287)(H,219,308)(H,220,309)(H,221,310)(H,225,267)(H,226,285)(H,227,295)(H,228,315)(H,229,269)(H,230,268)(H,231,270)(H,232,283)(H,233,282)(H,234,303)(H,235,290)(H,236,298)(H,237,300)(H,238,297)(H,239,296)(H,240,288)(H,241,292)(H,242,299)(H,243,289)(H,244,302)(H,245,307)(H,246,291)(H,247,301)(H,248,311)(H,249,312)(H,250,304)(H,251,271)(H,252,294)(H,253,306)(H,254,293)(H,255,305)(H,256,313)(H,257,284)(H,258,316)(H,259,314)(H,272,273)(H,274,275)(H,276,277)(H,278,279)(H,280,281)(H,317,318)(H4,210,211,215)/t106-,107-,108-,109-,110-,111-,112-,121-,122-,123-,124-,125-,126-,127-,128-,129-,130-,131-,132-,133-,134-,135-,136-,137-,138-,139-,140-,141-,142-,143-,158-,159-,160-,161-,162-,163-,164-,165-,166-/m0/s1

InChI Key

KMOIOFNRODJSOM-SIQRNXPUSA-N

Canonical SMILES

CCC(C)C(C(=O)NC(C(C)CC)C(=O)NCC(=O)NC(CC(C)C)C(=O)NC(CCSC)C(=O)NC(C(C)C)C(=O)NCC(=O)NCC(=O)NC(C(C)C)C(=O)NC(C(C)C)C(=O)NC(C(C)CC)C(=O)NC(C)C(=O)O)NC(=O)C(C)NC(=O)CNC(=O)C(CCCCN)NC(=O)C(CC(=O)N)NC(=O)C(CO)NC(=O)CNC(=O)C(C(C)C)NC(=O)C(CC(=O)O)NC(=O)C(CCC(=O)N)NC(=O)C(C)NC(=O)C(CC1=CC=CC=C1)NC(=O)C(CC2=CC=CC=C2)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CCCCN)NC(=O)C(CCC(=O)N)NC(=O)C(CC3=CN=CN3)NC(=O)C(CC4=CN=CN4)NC(=O)C(C(C)C)NC(=O)C(CCC(=O)O)NC(=O)C(CC5=CC=C(C=C5)O)NC(=O)CNC(=O)C(CO)NC(=O)C(CC(=O)O)NC(=O)C(CC6=CN=CN6)NC(=O)C(CCCNC(=N)N)NC(=O)C(CC7=CC=CC=C7)NC(=O)C(CCC(=O)O)NC(=O)C(C)NC(=O)C(CC(=O)O)N

1. Toxicity of various amyloid beta peptide species in cultured human blood-brain barrier endothelial cells: increased toxicity of dutch-type mutant

P B Eisenhauer, R J Johnson, J M Wells, T A Davies, R E Fine J Neurosci Res. 2000 Jun 15;60(6):804-10. doi: 10.1002/1097-4547(20000615)60:63.0.CO;2-1.

The amyloid beta peptide (A beta) is the major component of the neuritic and cerebrovascular amyloid plaques that are one of the characteristic features of Alzheimer's disease (AD). This peptide has been shown to be toxic to several relevant cell types, including neurons, cerebrovascular smooth muscle cells, and endothelial cells. We have studied the toxic effects of both soluble and aggregated species of A beta(1-40) and the mutation A beta(1-40)Glu-->Gln(22), which is the major species deposited in the cerebrovascular blood vessels of victims of hereditary cerebral hemorrhage with amyloidosis, Dutch type. We find that aggregates of both peptides, as well as of A beta(1-42) and A beta(25-35), are toxic to cultured human cerebrovascular endothelial cells (hBEC) obtained from the brain of a victim of AD (at doses lower than those that are toxic to CNS neurons or leptomeningeal smooth muscle cells). Soluble A beta(1-40) Gln(22) is equally toxic to hBEC, whereas wild-type A beta(1-40) is toxic only at higher doses. This toxicity is seen at the lowest dose of A beta(1-40) Gln (22) used, 20 nM. The soluble A beta(1-40)Gln(22) aggregates on the surface of the cells, in contrast to A beta(1-40), and its toxicity can be blocked both by an inhibitor of free radical formation and by Congo red, which inhibits amyloid fibril formation. We discuss the possibility that the enhanced toxicity of A beta(1-40)Gln(22) is mediated by a A beta receptor on the endothelial cells.

2. Amyloid beta-peptide1-42 alters tight junction protein distribution and expression in brain microvessel endothelial cells

Sonia Marco, Stephen D Skaper Neurosci Lett. 2006 Jul 3;401(3):219-24. doi: 10.1016/j.neulet.2006.03.047. Epub 2006 Apr 27.

Alzheimer's disease is characterised by neuronal loss, numerous intraneuronal deposits of neurofibrillary tangles, senile plaques, and cerebrovascular amyloid deposits. The major component of senile plaques and cerebrovascular deposits is the 39-43 amino acid beta-amyloid peptide (Abeta). The effects of Abeta on cerebral endothelium and thus the blood-brain barrier remain unclear. Utilising endothelial cells isolated from rat cerebral cortex microvessels, we have examined effects of Abeta peptides on tight junction protein behaviour. The transmembrane tight junction proteins occludin, claudin-1 and claudin-5, as well as the cytoplasmic accessory proteins ZO-1 and ZO-2 displayed a continuous distribution at cell boundaries. Endothelial cells exposed to Abeta1-42 (20 microM) for 3 days showed a disrupted plasma membrane pattern of claudin-5 and ZO-2 with relocation to the cytoplasm. These effects were not seen with Abeta25-35 or Abeta1-40[Gln22] (Dutch type). Abeta1-42 treatment altered also protein expression: occludin was lower at 1st day, claudin-1 increased at all times, and ZO-2 increased after 1 day and then decreased. These data suggest that Abeta1-42 effects on tight junction protein complexes may alter blood-brain barrier integrity and contribute to the neuropathological sequelae of Alzheimer's disease.

3. Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate

D M Walsh, A Lomakin, G B Benedek, M M Condron, D B Teplow J Biol Chem. 1997 Aug 29;272(35):22364-72. doi: 10.1074/jbc.272.35.22364.

Fibrillogenesis of the amyloid beta-protein (Abeta) is a seminal pathogenetic event in Alzheimer's disease. Inhibiting fibrillogenesis is thus one approach toward disease therapy. Rational design of fibrillogenesis inhibitors requires elucidation of the stages and kinetics of Abeta fibrillogenesis. We report results of studies designed to examine the initial stages of Abeta oligomerization. Size exclusion chromatography, quasielastic light scattering spectroscopy, and electron microscopy were used to characterize fibrillogenesis intermediates. After dissolution in 0.1 M Tris-HCl, pH 7.4, and removal of pre-existent seeds, Abeta chromatographed almost exclusively as a single peak. The molecules composing the peak had average hydrodynamic radii of 1.8 +/- 0.2 nm, consistent with the predicted size of dimeric Abeta. Over time, an additional peak, with a molecular weight >100,000, appeared. This peak contained predominantly curved fibrils, 6-8 nm in diameter and <200 nm in length, which we have termed "protofibrils." The kinetics of protofibril formation and disappearance are consistent with protofibrils being intermediates in the evolution of amyloid fibers. Protofibrils appeared during the polymerization of Abeta-(1-40), Abeta-(1-42), and Abeta-(1-40)-Gln22, peptides associated with both sporadic and inherited forms of Alzheimer's disease, suggesting that protofibril formation may be a general phenomenon in Abeta fibrillogenesis. If so, protofibrils could be attractive targets for fibrillogenesis inhibitors.