A 24-residue amyloid-β protein fragment
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Amyloid-β (17-40) Peptide (human) (trifluoroacetate salt)

Item No. 27414

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
L-leucyl-L-valyl-L-phenylalanyl-L-phenylalanyl-L-alanyl-L-α-glutamyl-L-α-aspartyl-L-valylglycyl-L-seryl-L-asparaginyl-L-lysylglycyl-L-alanyl-L-isoleucyl-L-L-isoleucylglycyl-L-leucyl-L-methionyl-L-valylglycylglycyl-L-valyl-L-valine
Synonyms
  • Aβ (17-40)
Molecular Formula
C110H178N26O31S • XCF3COOH
Formula Weight
2392.8
Purity
≥95%
Formulation (Request formulation change)
A solid
Solubility(Learn about Variance in Solubility)
Formic Acid: 1 mg/ml
SMILES
[H]N[C@@H](CC(C)C)C(N[C@@H](C(C)C)C(N[C@H](C(N[C@H](C(N[C@H](C(N[C@@H](CCC(O)=O)C(N[C@H](C(N[C@@H](C(C)C)C(NCC(N[C@@H](CO)C(N[C@@H](CC(N)=O)C(N[C@@H](CCCCN)C(NCC(N[C@H](C(N[C@]([C@H](CC)C)([H])C(N[C@]([C@H](CC)C)([H])C(NCC(N[C@@H](CC(C)C)C(N[C@H](C(N[C@@H](C(C)C)C(NCC(NCC(N[C@@H](C(C)C)C(N[C@@H](C(C)C)C(O)=O)=O)=O)=O)=O)=O)CCSC)=O)=O)=O)=O)=O)C)=O)=O)=O)=O)=O)=O)=O)CC(O)=O)=O)=O)C)=O)CC1=CC=CC=C1)=O)CC2=CC=CC=C2)=O)=O.O=C(O)C(F)(F)F
InChi Code
InChI=1S/C110H178N26O31S.C2HF3O2/c1-22-61(17)90(106(162)118-51-80(141)121-71(43-55(5)6)99(155)125-70(39-41-168-21)97(153)132-85(56(7)8)104(160)116-48-78(139)114-49-82(143)130-87(58(11)12)108(164)134-89(60(15)16)110(166)167)136-109(165)91(62(18)23-2)135-93(149)63(19)119-79(140)50-115-95(151)68(36-30-31-40-111)124-101(157)74(46-77(113)138)127-103(159)76(53-137)122-81(142)52-117-105(161)86(57(9)10)133-102(158)75(47-84(146)147)128-96(152)69(37-38-83(144)145)123-92(148)64(20)120-98(154)72(44-65-32-26-24-27-33-65)126-100(156)73(45-66-34-28-25-29-35-66)129-107(163)88(59(13)14)131-94(150)67(112)42-54(3)4;3-2(4,5)1(6)7/h24-29,32-35,54-64,67-76,85-91,137H,22-23,30-31,36-53,111-112H2,1-21H3,(H2,113,138)(H,114,139)(H,115,151)(H,116,160)(H,117,161)(H,118,162)(H,119,140)(H,120,154)(H,121,141)(H,122,142)(H,123,148)(H,124,157)(H,125,155)(H,126,156)(H,127,159)(H,128,152)(H,129,163)(H,130,143)(H,131,150)(H,132,153)(H,133,158)(H,134,164)(H,135,149)(H,136,165)(H,144,145)(H,146,147)(H,166,167);(H,6,7)/t61-,62-,63-,64-,67-,68-,69-,70-,71-,72-,73-,74-,75-,76-,85-,86-,87-,88-,89-,90-,91-;/m0./s1
InChi Key
WZWGWWUJGSVIBR-AZDDCZEESA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    1 mg

    $448

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    Product Description

    Amyloid-β (Aβ) (17-40) is a 24-residue fragment of the Aβ protein that is formed via post-translational processing of amyloid precursor protein (APP) by α- and γ-secretases.1 In vitro, Aβ (17-40) polymerizes into lattice-like structures that do not bind thioflavin T. It inhibits interactions between fibrinogen and biotinylated Aβ (1-42) (Item No. 27410) as well as between cholesterol and apolipoprotein E (ApoE) with IC50 values of 13.4 and 25 μM, respectively.2,3 Aβ (17-40) increases the rate of Aβ (1-40) (Item No. 21617) aggregation in vitro when used at an equimolar concentration.4 Aβ (17-40) (25 μM) induces cell death in cultured rat hippocampal neurons.5

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Näslund, J., Jensen, M., Tjernberg, L.O., et al. The metabolic pathway generating p3, an Aβ-peptide fragment, is probably non-amyloidogenic. Biochem. Biophys. Res. Commun. 204(2), 780-787 (1994).

    2. Zamolodchikov, D., Berk-Rauch, H.E., Oren, D.A., et al. Biochemical and structural analysis of the interaction between β-amyloid and fibrinogen. Blood 128(8), 1144-1151 (2016).

    3. Yao, Z.X., and Papadopoulos, V. Function of β-amyloid in cholesterol transport: A lead to neurotoxicity. The FASEB Journal 16(12), 1677-1679 (2002).

    4. Liu, R., McAllister, C., Lyubchenko, Y., et al. Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation. J. Neurosci. Res. 75(2), 162-171 (2004).

    5. Pike, C.J., Overman, M.J., and Cotman, C.W. Amino-terminal deletions enhance aggregation of β-amyloid peptides in vitro. The Journal of Biological Chemisty 270(41), 23895-23898 (1995).