Inhibition of GNNQQNY prion peptide aggregation by trehalose: a mechanistic view

Acyclic β-hairpins designed on oligomeric and fibril structures of Aβ1–42 disrupt protein–protein interactions mediating amyloid β-peptide aggregation.

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Poster: In silico hypotheses of the Aβ42 peptide aggregation process in Alzheimer's disease

2011 IEEE 1st International Conference on Computational Advances in Bio and Medical Sciences (ICCABS) ◽

10.1109/iccabs.2011.5729897 ◽

2011 ◽

Author(s):

Preetam Ghosh ◽

Bhaswati Datta ◽

Vijayaraghavan Rangachari

Keyword(s):

Alzheimer’S Disease ◽

Alzheimer's Disease ◽

In Silico ◽

Peptide Aggregation ◽

Aggregation Process

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

Chemical Communications ◽

10.1039/c4cc09063b ◽

2015 ◽

Vol 51 (12) ◽

pp. 2245-2248 ◽

Cited By ~ 36

Author(s):

Ashim Paul ◽

Krishna Chaitanya Nadimpally ◽

Tanmay Mondal ◽

Kishore Thalluri ◽

Bhubaneswar Mandal

Keyword(s):

Anthranilic Acid ◽

Amyloid Β ◽

Amyloid Β Peptide ◽

Peptide Aggregation ◽

Hybrid Peptide ◽

Conformationally Restricted ◽

Β Sheet

A novel class of anthranilic acid containing a conformationally restricted β-sheet breaker α/β-hybrid peptide efficiently disrupts preformed fibrillar aggregates of Aβ1–40in vitro.

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The use of 4,4,4-trifluorothreonine to stabilize extended peptide structures and mimic β-strands

Beilstein Journal of Organic Chemistry ◽

10.3762/bjoc.13.276 ◽

2017 ◽

Vol 13 ◽

pp. 2842-2853 ◽

Cited By ~ 1

Author(s):

Yaochun Xu ◽

Isabelle Correia ◽

Tap Ha-Duong ◽

Nadjib Kihal ◽

Jean-Louis Soulier ◽

...

Keyword(s):

Protein Interactions ◽

Amyloid Peptide ◽

Central Position ◽

Aggregation Process ◽

Proof Of Concept ◽

Protein Protein Interactions ◽

Conformational Studies ◽

Dynamics Simulations ◽

Β Sheet ◽

Central Residue

Pentapeptides having the sequence R-HN-Ala-Val-X-Val-Leu-OMe, where the central residue X is L-serine, L-threonine, (2S,3R)-L-CF3-threonine and (2S,3S)-L-CF3-threonine were prepared. The capacity of (2S,3S)- and (2S,3R)-CF3-threonine analogues to stabilize an extended structure when introduced in the central position of pentapeptides is demonstrated by NMR conformational studies and molecular dynamics simulations. CF3-threonine containing pentapeptides are more prone to mimic β-strands than their natural Ser and Thr pentapeptide analogues. The proof of concept that these fluorinated β-strand mimics are able to disrupt protein–protein interactions involving β-sheet structures is provided. The CF3-threonine containing pentapeptides interact with the amyloid peptide Aβ1-42 in order to reduce the protein–protein interactions mediating its aggregation process.

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