Aβ_1–42 C-terminus fragment derived peptides prevent the self-assembly of the parent peptide

Abstract

A series of peptides derived from the C-terminus fragment (Aβ38–42) of Aβ showed significant to complete reduction in Aβ-induced toxicity.

Effect of C-terminus amidation of Aβ39–42fragment derived peptides as potential inhibitors of Aβ aggregation

“…Upon the basis of careful analysis of data reported herewith and results published earlier, [10][11][12] a correlation between the amino acid residues within the tetrapeptide sequence and the exhibited activity was established. Replacement of the rst residue, Val 39 with hydrophobic residues (Phe and D-Phe) exhibited >90% inhibition.…”

“…Studies on a complete peptide scan on the C-terminus region regions has already been published previously. [10][11][12] In an attempt to enhance the biological efficacy of the previously designed scaffolds, 12 we rationalized the use of sequential amino acid scan by modifying/replacing individual residues, as well as amide protection of the Cterminus on the lead tetrapeptide sequence (Val-Val-Ile-Ala) to enhance the proteolytic stability of the peptides.…”

“…To understand the interaction of the test peptide with the full-length Ab 42 , a grid incorporating the whole sequence was generated. Docking studies were performed with the peptides mentioned in this work along with a few molecules reported in literature [10][11][12]55,56 for comparative analysis of the binding modes and interactions. [57][58][59] Docking, glide and residual interaction energy scores for the molecules selected from literature and test peptides from the current study are summarized in ESI (Tables S9 and S10 †).…”

C-Terminal Fragment, Aβ39–42-Based Tetrapeptides Mitigates Amyloid-β Aggregation-Induced Toxicity

“…Fragments Aβ 31–42 , Aβ 38–42 , and Aβ 39–42 derived from the hydrophobic C-terminus region were found to reduce the Aβ aggregation significantly . A recent report investigated the inhibitory effects of pentapeptides derived from the fragment Aβ 38–42 . A number of peptides were discovered to exhibit significant to complete inhibition of Aβ 1–42 aggregation.…”

“…37 A recent report investigated the inhibitory effects of pentapeptides derived from the fragment Aβ 38−42 . 38 A number of peptides were discovered to exhibit significant to complete inhibition of Aβ 1−42 aggregation. In another study, N-methylation performed on the hexapeptide fragment, Aβ 32−37 was shown to afford efficient inhibitors of Aβ aggregation.…”