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Application Area

Amyloid β-Protein (11-42)

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

Category

Functional Peptides

Catalog number

BAT-014628

CAS number

157802-70-5

Molecular Formula

C152H244N40O42S

Molecular Weight

3335.87

Specification
Reference Reading

IUPAC Name

(4S)-4-amino-5-[[(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)-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]-4-carboxy-1-oxobutan-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-4-yl)-1-oxopropan-2-yl]amino]-3-(1H-imidazol-4-yl)-1-oxopropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-5-oxopentanoic acid

Synonyms

β Amyloid (11-42); H-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; L-alpha-glutamyl-L-valyl-L-histidyl-L-histidyl-L-glutaminyl-L-lysyl-L-leucyl-L-valyl-L-phenylalanyl-L-phenylalanyl-L-alanyl-L-alpha-glutamyl-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 Lyophilized Powder

Purity

≥95%

Sequence

EVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA

Storage

Store at -20°C

Solubility

Soluble in DMSO, Water

InChI

InChI=1S/C152H244N40O42S/c1-27-82(20)123(145(226)164-69-111(198)170-98(56-74(4)5)135(216)176-97(52-55-235-26)133(214)186-117(76(8)9)143(224)162-66-109(196)160-67-113(200)184-119(78(12)13)148(229)189-122(81(18)19)149(230)192-124(83(21)28-2)150(231)169-87(25)152(233)234)191-151(232)125(84(22)29-3)190-127(208)85(23)167-110(197)68-161-129(210)93(44-36-38-53-153)173-139(220)104(62-108(157)195)180-142(223)106(71-193)171-112(199)70-163-144(225)118(77(10)11)187-141(222)105(63-116(205)206)181-132(213)96(48-51-115(203)204)172-126(207)86(24)168-134(215)100(58-88-40-32-30-33-41-88)178-136(217)101(59-89-42-34-31-35-43-89)182-147(228)121(80(16)17)188-140(221)99(57-75(6)7)177-130(211)94(45-37-39-54-154)174-131(212)95(47-49-107(156)194)175-137(218)102(60-90-64-158-72-165-90)179-138(219)103(61-91-65-159-73-166-91)183-146(227)120(79(14)15)185-128(209)92(155)46-50-114(201)202/h30-35,40-43,64-65,72-87,92-106,117-125,193H,27-29,36-39,44-63,66-71,153-155H2,1-26H3,(H2,156,194)(H2,157,195)(H,158,165)(H,159,166)(H,160,196)(H,161,210)(H,162,224)(H,163,225)(H,164,226)(H,167,197)(H,168,215)(H,169,231)(H,170,198)(H,171,199)(H,172,207)(H,173,220)(H,174,212)(H,175,218)(H,176,216)(H,177,211)(H,178,217)(H,179,219)(H,180,223)(H,181,213)(H,182,228)(H,183,227)(H,184,200)(H,185,209)(H,186,214)(H,187,222)(H,188,221)(H,189,229)(H,190,208)(H,191,232)(H,192,230)(H,201,202)(H,203,204)(H,205,206)(H,233,234)/t82-,83-,84-,85-,86-,87-,92-,93-,94-,95-,96-,97-,98-,99-,100-,101-,102-,103-,104-,105-,106-,117-,118-,119-,120-,121-,122-,123-,124-,125-/m0/s1

InChI Key

RTKFLMQQZOPJCC-TZSBUWKVSA-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)O)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=CNC=N3)NC(=O)C(CC4=CNC=N4)NC(=O)C(C(C)C)NC(=O)C(CCC(=O)O)N

1. Structural analysis of the Aβ(11-42) amyloid fibril based on hydrophobicity distribution

Irena Roterman, Dawid Dułak, Małgorzata Gadzała, Mateusz Banach, Leszek Konieczny J Comput Aided Mol Des. 2019 Jul;33(7):665-675. doi: 10.1007/s10822-019-00209-9. Epub 2019 Jul 10.

The structure of the Aβ(11-42) amyloid available in PDB makes possible the molecular analysis of the specificity of amyloid formation. This molecule (PDB ID 2MVX) is the object of analysis. This work presents the outcome of in silico experiments involving various alternative conformations of the Aβ(11-42) sequence, providing clues as to the amylodogenecity of its constituent fragments. The reference structure (PDB) has been compared with folds generated using I-Tasser and Robetta-the strongest contenders in the CASP challenge. Additionally, a polypeptide which matches the Aβ(11-42) sequence has been subjected to folding simulations based on the fuzzy oil drop model, which favors the production of a monocentric hydrophobic core. Computer simulations yielded 15 distinct structural forma (five per software package), which, when compared to the experimentally determined structure, allow us to study the role of structural elements which cause an otherwise globular protein to transform into an amyloid. The unusual positions of hydrophilic residues disrupting the expected hydrophobic core and propagating linearly along the long axis of fibril is recognized as the seed for amyloidogenic transformation in this polypeptide. This paper discusses the structure of the Aβ(11-42) amyloid fibril, listed in PDB under ID 2MXU (fragment od Aβ(1-42) amyloid).

2. Truncated Amyloid-β(11-40/42) from Alzheimer Disease Binds Cu2+ with a Femtomolar Affinity and Influences Fiber Assembly

Joseph D Barritt, John H Viles J Biol Chem. 2015 Nov 13;290(46):27791-802. doi: 10.1074/jbc.M115.684084. Epub 2015 Sep 25.

Alzheimer disease coincides with the formation of extracellular amyloid plaques composed of the amyloid-β (Aβ) peptide. Aβ is typically 40 residues long (Aβ(1-40)) but can have variable C and N termini. Naturally occurring N-terminally truncated Aβ(11-40/42) is found in the cerebrospinal fluid and has a similar abundance to Aβ(1-42), constituting one-fifth of the plaque load. Based on its specific N-terminal sequence we hypothesized that truncated Aβ(11-40/42) would have an elevated affinity for Cu(2+). Various spectroscopic techniques, complemented with transmission electron microscopy, were used to determine the properties of the Cu(2+)-Aβ(11-40/42) interaction and how Cu(2+) influences amyloid fiber formation. We show that Cu(2+)-Aβ(11-40) forms a tetragonal complex with a 34 ± 5 fm dissociation constant at pH 7.4. This affinity is 3 orders of magnitude tighter than Cu(2+) binding to Aβ(1-40/42) and more than an order of magnitude tighter than that of serum albumin, the extracellular Cu(2+) transport protein. Furthermore, Aβ(11-40/42) forms fibers twice as fast as Aβ(1-40) with a very different morphology, forming bundles of very short amyloid rods. Substoichiometric Cu(2+) drastically perturbs Aβ(11-40/42) assembly, stabilizing much longer fibers. The very tight fm affinity of Cu(2+) for Aβ(11-40/42) explains the high levels of Cu(2+) observed in Alzheimer disease plaques.

3. Investigation of the interaction of amyloid β peptide (11-42) oligomers with a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) membrane using molecular dynamics simulation

Ning Xiang, Yuan Lyu, Xiao Zhu, Ganesan Narsimhan Phys Chem Chem Phys. 2018 Mar 7;20(10):6817-6829. doi: 10.1039/c7cp07148e.

Some amyloid related proteins/peptides are involved in aggregation and pore formation in phospholipid membranes (cell membranes), which result in a variety of neurological disorders such as Alzheimer's disease, Parkinson's disease and Huntington disease. In this research, the mechanism of pore formation by β amyloid (Aβ) peptides was investigated using molecular dynamics simulation by simulating the interaction of the Aβ(11-42) peptide, with a lipid membrane and the potential of the mean force of interaction was evaluated. A 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) membrane system with different cholesterol concentrations was used to simulate the neural cell membrane. The results indicated that Aβ(11-42) peptide oligomers with peptide numbers larger than two were more likely to lead to lipid deformation and water channels, and the free energy of penetration into the membrane decreased with the increasing number of peptides. Increasing the concentration of cholesterol leads to a higher energy barrier for the penetration of peptide into the lipid bilayer thereby protecting the membrane. The results of this research have potential application in the prevention of pore formation by Aβ aggregates on the lipid membrane.