mutation

β-Amyloid (1-40), England mutation, is a biologically active peptide with a histidine (His) to arginine (Arg) substitution at position 6, known to enhance oligomerization kinetics that serve as fibril seeds and increase neurotoxicity in cultured neurons. This alteration is one of several mutations in the beta-amyloid precursor gene implicated in autosomal dominant Alzheimer's Disease across multiple kindreds.

[Arg6]-β-Amyloid (1-42), England mutation, is a biologically active peptide linked to autosomal dominant Alzheimer's Disease in various kindreds. The English (H6R) mutation disrupts H6 interactions due to alterations in the beta-amyloid precursor gene.

[Asn23] β-Amyloid (1-40), Iowa mutation, is a biologically active peptide linked to autosomal dominant Alzheimer's Disease in multiple families. This involves the substitution of Asp 23 with Asn, causing severe cerebral amyloid beta-protein angiopathy (CAA). Individuals with this mutation exhibit a missense alteration in the APP gene at position 694, resulting in the mutated β-amyloid peptide aggregating more quickly and forming toxic fibrils.

[Asn23]-beta-Amyloid (1-42), Iowa mutation, is a biologically active peptide with increased aggregation propensity and fibril toxicity. This mutation involves the substitution of Aspartic acid (Asp) at position 23 with Asparagine (Asn), contributing to autosomal dominant Alzheimer's Disease and associated with severe cerebral amyloid beta-protein angiopathy (CAA) due to a missense alteration at position 694 of the amyloid precursor protein (APP) gene.

EGFRvIII peptide PEPvIII acetate is a tumor-specific mutation that is widely expressed in glioblastoma multiforme (GBM) and other neoplasms and enhances tumorigenicity.

(Gly22)-Amyloid β-Protein (1-42), a peptide fragment of Amyloid β-Protein (Aβ), plays a crucial role in Alzheimer's disease by forming the main component of vascular and parenchymal amyloid deposits. The Glu22 to Gly22 mutation in Aβ is known to enhance aggregation [1] [2].

Tat-NR2BAA TFA serves as the inactive control peptide for Tat-NR2B9c, featuring a comparable sequence with a crucial distinction: a double-point mutation in its COOH-terminal tSXV motif. This alteration renders Tat-NR2BAA TFA unable to bind to PSD-95, in contrast to Tat-NR2B9c. The latter is a membrane-permeant peptide that impedes PSD-95/NMDAR interaction, specifically detaching NR2B- and/or NR2A-type NMDARs from PSD-95 [1].

'(Lys22)-Amyloid β-Protein (1-42) represents a mutation of the wild-type (WT) Amyloid β-Protein (1-42) peptide [1].'

(Gln22)-Amyloid β-Protein (1-42), a Dutch mutation (E22Q) variant of β-Amyloid (1-42), exhibits enhanced fibrillogenic and pathogenic properties [1].

E70K is a compound that inhibits the interaction between the chemokine (C-X-C) ligand 8 (CXCL8) and glycosaminoglycans (GAGs) on cell membrane surfaces. It mimics a segment of the CXCL8 protein's GAG-binding region at the C-terminal end, incorporating a glutamate-to-lysine mutation at the 70th position. At a concentration of 50 nM, E70K notably reduces the attachment of primary human neutrophils to human umbilical vein endothelial cells (HUVECs). Moreover, it impedes the CXCL8-triggered movement of these neutrophils across HMEC-1 human microvascular endothelial cell layers within a concentration range of 1 to 1,000 nM.

M-2420 is a fluorogenic substrate specifically designed for the β-secretase site associated with the Swedish mutation of the amyloid precursor protein (APP).

(Glu20)-Amyloid β-Protein (1-42) represents a variant of amyloid β-protein (Aβ) that fibrillizes more slowly due to the Glu20 mutation, which diminishes Aβ42's tendency to aggregate and inhibits the accumulation of this slowly fibrillizing peptide. Amyloid β-protein is the principal constituent of amyloid deposits in the vascular system and brain parenchyma in Alzheimer's disease [1] [2].

Rhodopsin peptide is a peptide with the sequence H2N-Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala-OH, MW= 1217.33. Rhodopsin is a biological pigment in photoreceptor cells of the retina that is responsible for the first events in the perception of ligh

KRAS G13D peptide, a 25-mer sequence, is derived from the KRAS activating oncogene mutation and serves as an immune potentiator. This peptide possesses immunogenic properties and can be utilized for the development of a KRAS vaccine.

Tat-NR2BAA is an inactive control peptide of Tat-NR2B9c. It shares a similar sequence with Tat-NR2B9c, but possesses a double-point mutation in the COOH terminal tSXV motif. This mutation renders Tat-NR2BAA unable to bind PSD-95. Tat-NR2B9c, on the other hand, is a membrane-permeable peptide that interferes with PSD-95 NMDAR binding. This interference leads to the decoupling of NR2B- and or NR2A-type NMDARs from PSD-95[1][2].