Need Assistance?

US & Canada:
+
UK: +

Our Highlights

GMP Grade Efficient workshop for GMP production.
Optimal Prices Buying products on this site guarantees the best price!
Commercial Batches Independent GMP manufacturing suites that handle commercial batches
Prompt Delivery Warehouses in multiple cities to ensure timely delivery
Flexible Quantity Quantities available from milligrams to ton

Amyloid β-Protein (3-42)

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

With the development of AD, N-terminal truncation of Aβ42 may be formed in increased amounts. Amyloid β-Protein (3-42) is a precursor of Pyr-peptide. The resistance of (Pyr3)-Aβ 3-42 positive plaque to age-dependent degradation may be due to its high stability and aggregation tendency.

Category

Functional Peptides

Catalog number

BAT-014666

CAS number

157884-74-7

Molecular Formula

C196H301N53O56S

Molecular Weight

4327.94

Specification
Reference Reading

IUPAC Name

(4S)-4-amino-5-[[(1S)-2-[[(1S)-1-[[(1S)-2-[[(1S)-2-[[(1S)-2-[[2-[[(1S)-2-[[(1S)-1-[[(1S)-1-[[(1S)-2-[[(1S)-2-[[(1S)-4-amino-1-[[(1S)-5-amino-1-[[(1S)-1-[[(1S)-1-[[(1S)-2-[[(1S)-2-[[(1S)-2-[[(1S)-1-[[(1S)-2-[[(1S)-1-[[2-[[(1S)-2-[[(1S)-3-amino-1-[[(1S)-5-amino-1-[[2-[[(1S)-2-[[(1S,2S)-1-[[(1S,2S)-1-[[2-[[(1S)-1-[[(1S)-1-[[(1S)-1-[[2-[[2-[[(1S)-1-[[(1S)-1-[[(1S,2S)-1-[[(1S)-1-carboxyethyl]carbamoyl]-2-methyl-butyl]carbamoyl]-2-methyl-propyl]carbamoyl]-2-methyl-propyl]amino]-2-oxo-ethyl]amino]-2-oxo-ethyl]carbamoyl]-2-methyl-propyl]carbamoyl]-3-methylsulfanyl-propyl]carbamoyl]-3-methyl-butyl]amino]-2-oxo-ethyl]carbamoyl]-2-methyl-butyl]carbamoyl]-2-methyl-butyl]amino]-1-methyl-2-oxo-ethyl]amino]-2-oxo-ethyl]carbamoyl]pentyl]carbamoyl]-3-oxo-propyl]amino]-1-(hydroxymethyl)-2-oxo-ethyl]amino]-2-oxo-ethyl]carbamoyl]-2-methyl-propyl]amino]-1-(carboxymethyl)-2-oxo-ethyl]carbamoyl]-3-carboxy-propyl]amino]-1-methyl-2-oxo-ethyl]amino]-1-benzyl-2-oxo-ethyl]amino]-1-benzyl-2-oxo-ethyl]carbamoyl]-2-methyl-propyl]carbamoyl]-3-methyl-butyl]carbamoyl]pentyl]carbamoyl]-4-oxo-butyl]amino]-1-(1H-imidazol-4-ylmethyl)-2-oxo-ethyl]amino]-1-(1H-imidazol-4-ylmethyl)-2-oxo-ethyl]carbamoyl]-2-methyl-propyl]carbamoyl]-3-carboxy-propyl]amino]-1-[(4-hydroxyphenyl)methyl]-2-oxo-ethyl]amino]-2-oxo-ethyl]amino]-1-(hydroxymethyl)-2-oxo-ethyl]amino]-1-(carboxymethyl)-2-oxo-ethyl]amino]-1-(1H-imidazol-4-ylmethyl)-2-oxo-ethyl]carbamoyl]-4-guanidino-butyl]amino]-1-benzyl-2-oxo-ethyl]amino]-5-oxo-pentanoic acid

Synonyms

Aβ (3-42); H-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala-OH

Appearance

White Powder

Purity

≥95%

Sequence

EFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA

Storage

Store at -20°C

Solubility

Soluble in Acetic Acid, DMSO; Insoluble in DMF, Water

InChI

InChI=1S/C196H301N53O56S/c1-27-104(20)159(188(297)213-89-145(258)220-126(70-96(4)5)174(283)229-125(65-69-306-26)172(281)242-153(98(8)9)186(295)211-85-142(255)208-86-147(260)241-155(100(12)13)191(300)246-158(103(18)19)192(301)249-160(105(21)28-2)193(302)219-109(25)195(304)305)248-194(303)161(106(22)29-3)247-163(272)107(23)217-143(256)87-209-165(274)119(50-39-41-66-197)224-181(290)135(79-141(201)254)235-185(294)139(92-251)222-146(259)90-212-187(296)154(99(10)11)243-184(293)137(81-152(269)270)236-170(279)123(59-63-149(263)264)223-162(271)108(24)218-173(282)129(72-110-44-33-30-34-45-110)232-177(286)131(74-112-48-37-32-38-49-112)238-189(298)157(102(16)17)245-183(292)127(71-97(6)7)231-167(276)120(51-40-42-67-198)225-169(278)122(58-61-140(200)253)227-178(287)132(76-114-82-204-93-214-114)234-180(289)134(78-116-84-206-95-216-116)239-190(299)156(101(14)15)244-171(280)124(60-64-150(265)266)228-175(284)128(75-113-53-55-117(252)56-54-113)221-144(257)88-210-166(275)138(91-250)240-182(291)136(80-151(267)268)237-179(288)133(77-115-83-205-94-215-115)233-168(277)121(52-43-68-207-196(202)203)226-176(285)130(73-111-46-35-31-36-47-111)230-164(273)118(199)57-62-148(261)262/h30-38,44-49,53-56,82-84,93-109,118-139,153-161,250-252H,27-29,39-43,50-52,57-81,85-92,197-199H2,1-26H3,(H2,200,253)(H2,201,254)(H,204,214)(H,205,215)(H,206,216)(H,208,255)(H,209,274)(H,210,275)(H,211,295)(H,212,296)(H,213,297)(H,217,256)(H,218,282)(H,219,302)(H,220,258)(H,221,257)(H,222,259)(H,223,271)(H,224,290)(H,225,278)(H,226,285)(H,227,287)(H,228,284)(H,229,283)(H,230,273)(H,231,276)(H,232,286)(H,233,277)(H,234,289)(H,235,294)(H,236,279)(H,237,288)(H,238,298)(H,239,299)(H,240,291)(H,241,260)(H,242,281)(H,243,293)(H,244,280)(H,245,292)(H,246,300)(H,247,272)(H,248,303)(H,249,301)(H,261,262)(H,263,264)(H,265,266)(H,267,268)(H,269,270)(H,304,305)(H4,202,203,207)/t104-,105-,106-,107-,108-,109-,118-,119-,120-,121-,122-,123-,124-,125-,126-,127-,128-,129-,130-,131-,132-,133-,134-,135-,136-,137-,138-,139-,153-,154-,155-,156-,157-,158-,159-,160-,161-/m0/s1

InChI Key

KKTVQBBKTFSAGX-SUJODTBGSA-N

1. Aggregation States of A β1-40, A β1-42 and A β p3-42 Amyloid Beta Peptides: A SANS Study

Giulia Festa, et al. Int J Mol Sci. 2019 Aug 24;20(17):4126. doi: 10.3390/ijms20174126.

Aggregation states of amyloid beta peptides for amyloid beta A β 1 - 40 to A β 1 - 42 and A β p 3 - 42 are investigated through small angle neutron scattering (SANS). The knowledge of these small peptides and their aggregation state are of key importance for the comprehension of neurodegenerative diseases (e.g., Alzheimer's disease). The SANS technique allows to study the size and fractal nature of the monomers, oligomers and fibrils of the three different peptides. Results show that all the investigated peptides have monomers with a radius of gyration of the order of 10 Å, while the oligomers and fibrils display differences in size and aggregation ability, with A β p 3 - 42 showing larger oligomers. These properties are strictly related to the toxicity of the corresponding amyloid peptide and indeed to the development of the associated disease.

2. Solid-phase synthesis and pathological evaluation of pyroglutamate amyloid-β3-42 peptide

Illhwan Cho, HeeYang Lee, Donghee Lee, In Wook Park, Soljee Yoon, Hye Yun Kim, YoungSoo Kim Sci Rep. 2023 Jan 10;13(1):505. doi: 10.1038/s41598-022-26616-x.

Pyroglutamate amyloid-β3-42 (AβpE3-42) is an N-terminally truncated and pyroglutamate-modified Aβ peptide retaining highly hydrophobic, amyloidogenic, and neurotoxic properties. In Alzheimer's disease (AD) patients, AβpE3-42 peptides accumulate into oligomers and induce cellular toxicity and synaptic dysfunction. AβpE3-42 aggregates further seed the formation of amyloid plaques, which are the pathological hallmarks of AD. Given that AβpE3-42 peptides play critical roles in the development of neurodegeneration, a reliable and reproducible synthetic access to these peptides may support pathological and medicinal studies of AD. Here, we synthesized AβpE3-42 peptides through the microwave-assisted solid-phase peptide synthesis (SPPS). Utilizing thioflavin T fluorescence assay and dot blotting analysis with anti-amyloid oligomer antibody, the amyloidogenic activity of synthesized AβpE3-42 peptides was confirmed. We further observed the cytotoxicity of AβpE3-42 aggregates in cell viability test. To examine the cognitive deficits induced by synthetic AβpE3-42 peptides, AβpE3-42 oligomers were intracerebroventricularly injected into imprinting control region mice and Y-maze and Morris water maze tests were performed. We found that AβpE3-42 aggregates altered the expression level of postsynaptic density protein 95 in cortical lysates. Collectively, we produced AβpE3-42 peptides in the microwave-assisted SPPS and evaluated the amyloidogenic and pathological function of the synthesized peptides.

3. Pyroglutamate-Modified Amyloid-β(3-42) Shows α-Helical Intermediates before Amyloid Formation

Christina Dammers, Kerstin Reiss, Lothar Gremer, Justin Lecher, Tamar Ziehm, Matthias Stoldt, Melanie Schwarten, Dieter Willbold Biophys J. 2017 Apr 25;112(8):1621-1633. doi: 10.1016/j.bpj.2017.03.007.

Pyroglutamate-modified amyloid-β (pEAβ) has been described as a relevant Aβ species in Alzheimer's-disease-affected brains, with pEAβ (3-42) as a dominant isoform. Aβ (1-40) and Aβ (1-42) have been well characterized under various solution conditions, including aqueous solutions containing trifluoroethanol (TFE). To characterize structural properties of pEAβ (3-42) possibly underlying its drastically increased aggregation propensity compared to Aβ (1-42), we started our studies in various TFE-water mixtures and found striking differences between the two Aβ species. Soluble pEAβ (3-42) has an increased tendency to form β-sheet-rich structures compared to Aβ (1-42), as indicated by circular dichroism spectroscopy data. Kinetic assays monitored by thioflavin-T show drastically accelerated aggregation leading to large fibrils visualized by electron microscopy of pEAβ (3-42) in contrast to Aβ (1-42). NMR spectroscopy was performed for backbone and side-chain chemical-shift assignments of monomeric pEAβ (3-42) in 40% TFE solution. Although the difference between pEAβ (3-42) and Aβ (1-42) is purely N-terminal, it has a significant impact on the chemical environment of >20% of the total amino acid residues, as revealed by their NMR chemical-shift differences. Freshly dissolved pEAβ (3-42) contains two α-helical regions connected by a flexible linker, whereas the N-terminus remains unstructured. We found that these α-helices act as a transient intermediate to β-sheet and fibril formation of pEAβ (3-42).