amyloid-beta-peptides and anthranilic-acid

amyloid-beta-peptides has been researched along with anthranilic-acid* in 1 studies

Other Studies

1 other study(ies) available for amyloid-beta-peptides and anthranilic-acid

Article	Year
Inhibition of Alzheimer's amyloid-β peptide aggregation and its disruption by a conformationally restricted α/β hybrid peptide. Chemical communications (Cambridge, England), 2015, Feb-11, Volume: 51, Issue:12 Insertion of an anthranilic acid in an amyloidogenic peptide sequence generates a novel conformationally restricted α/β-hybrid peptide that inhibits amyloid formation of Aβ(1-40) and disrupts preformed fibrillar aggregates in vitro. Such β-sheet breaker hybrid peptides (BSBHps) may be useful for designing novel physiologically important compounds relevant to diverse amyloidoses and for studying the process of aggregation. Topics: Alzheimer Disease; Amyloid beta-Peptides; Circular Dichroism; Humans; Microscopy, Electron, Transmission; ortho-Aminobenzoates; Peptide Fragments; Protein Binding; Protein Structure, Secondary	2015

Article

Year

Inhibition of Alzheimer's amyloid-β peptide aggregation and its disruption by a conformationally restricted α/β hybrid peptide.

Chemical communications (Cambridge, England), 2015, Feb-11, Volume: 51, Issue:12

Insertion of an anthranilic acid in an amyloidogenic peptide sequence generates a novel conformationally restricted α/β-hybrid peptide that inhibits amyloid formation of Aβ(1-40) and disrupts preformed fibrillar aggregates in vitro. Such β-sheet breaker hybrid peptides (BSBHps) may be useful for designing novel physiologically important compounds relevant to diverse amyloidoses and for studying the process of aggregation.

Topics: Alzheimer Disease; Amyloid beta-Peptides; Circular Dichroism; Humans; Microscopy, Electron, Transmission; ortho-Aminobenzoates; Peptide Fragments; Protein Binding; Protein Structure, Secondary

2015