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Results for "

β-sheet amyloids

" in MedChemExpress (MCE) Product Catalog:

6

Inhibitors & Agonists

8

Peptides

Cat. No. Product Name Target Research Area
  • HY-P10294
    Oligopeptide P11-4

    		Peptides Others
    Oligopeptide P11-4 is an α-peptide that can be self-assembled into β-sheet amyloids with a hydrogel appearance at low pH. Oligopeptide P11-4 can be used in biomimetic mineralization, enamel regeneration and oral care agent .
  • HY-P1047
    β-Sheet Breaker Peptide iAβ5

    [Pro18, Asp21] β-Amyloid (17-21)

    		 Amyloid-β Neurological Disease
    β-Sheet Breaker Peptide iAβ5 is an effective brain amyloid-β (Abeta) degrader. Abeta deposits are associated with Alzheimer's disease (AD), and the related toxicity arises from its β-sheet conformation and aggregation. β-Sheet Breaker Peptide iAβ5 can repeatedly induce the degradation of fibrillary amyloid deposits in vivo. Therefore, β-Sheet Breaker Peptide iAβ5 can prevent and/or reverse neuronal contraction caused by Abeta and reduce the range of interleukin IL-1beta positive microglial-like cells around Abeta deposits. β-Sheet Breaker Peptide iAβ5 can reduce the size and/or number of brain amyloid plaques in AD. β-Sheet Breaker Peptide iAβ5 is labeled with a hydrophobic benzyl alcohol (HBA) tag and shows a bright blue color under acidic conditions, which can be used for quantitative determination.
  • HY-P5905
    Citrullinated amyloid-β (1-42) peptide (human)

    Citrullinated Aβ (1-42); Citrullinated Aβ42

    		 Amyloid-β Neurological Disease
    Citrullinated amyloid-β (1-42) peptide (human) (Citrullinated Aβ (1-42)) is a modified form of β-Amyloid (1-42) (HY-P1363) with a citrullination at the Arg5 site. Compared to the unmodified β-Amyloid (1-42), its formation of soluble low-molecular-weight oligomers is enhanced, the rate of fibril formation is reduced, and like unmodified Aβ42, it forms protofibrils comprised of parallel β-sheets .
  • HY-P5967
    Acetly-β Amyloid(15-20), Amide

    		Peptides Neurological Disease
    Acetly-β Amyloid (15-20), Amide is a peptides fragment. Acetly-β Amyloid (15-20), Amide inhibits the β-sheet formation and stabilizes structure of Aβ (1–40) peptide. Acetly-β Amyloid (15-20), Amide can be used in study Alzheimer’s disease .
  • HY-P5515
    F(N-Me)GA(N-Me)IL

    		Peptides Others
    F(N-Me)GA(N-Me)IL is a biological active peptide. (Double N-methylated derivatives of amyloidogenic and cytotoxic partial IAPP sequence were found to be devoid of β-sheet structure, amyloidogenicity and cytotoxicity, The derivatives were able to interact with the native sequences and inhibit amyloid formation)
  • HY-P5906
    Citrullinated amyloid-β (1-40) peptide (human)

    Citrullinated Aβ (1-40); Citrullinated Aβ40

    		 Amyloid-β Neurological Disease
    Citrullinated amyloid-β (1-40) peptide (human) (Citrullinated Aβ (1-40)) is a modified form of β-Amyloid (1-40) (HY-P0265) with a citrullination at the Arg5 site. Citrullinated amyloid-β (1-40) peptide (human) exhibits increased transient formation of soluble oligomers and insoluble aggregates composed of distorted parallel β-sheets compared with unmodified β-Amyloid (1-40) .
  • HY-P4873
    Amylin (20-29) (human)

    		Peptides Neurological Disease
    Amylin (20-29) (human) is the fragment of human islet amyloid polypeptide (hIAPP) or Amylin. Amylin is a 37-residue hormone. Amylin (20-29) (human) is responsible for the amyloidogenic propensities of the full length protein. Amylin (20-29) (human) can be transformed into its corresponding peptoid and retropeptoid sequences, to obtain beta-sheet breaker peptides as amyloid inhibitors .
  • HY-P5340
    Amyloid-Forming peptide GNNQQNY

    		Peptides Others
    Amyloid-Forming peptide GNNQQNY is a biological active peptide. (This is a heptapeptide from the N-terminal prion-determining domain of the yeast protein Sup35 that forms amyloid fibrils. The availability of its detailed atomic oligomeric structure makes it a good model for studying the early stage of aggregation. The GNNQQNY dimer forms three stable sheet structures. in-register parallel, off-register parallel, and anti-parallel. The in-register parallel dimer, which is close to the amyloid beta-sheet structure, has few interpeptide hydrogen bonds, making hydrophobic interactions more important and increasing the conformational entropy compared to the anti-parallel sheet.)

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