Few Ramachandran Angle Changes Provide Interaction Strength Increase in Aβ42 versus Aβ40 Amyloid Fibrils

Oscar H. Bastidas, Benjamin Green, Mary Sprague, Michael H. Peters

Research output: Contribution to journalArticle

Abstract

The pathology of Alzheimer's disease can ultimately be traced to the increased aggregation stability of Aβ42 peptides which possess two extra residues (Ile 41 &Ala 42) that the non-pathological strain (Aβ40) lacks. We have found Aβ42 fibrils to exhibit stronger energies in inter-chain interactions and we have also identified the cause for this increase to be the result of different Ramachandran angle values in certain residues of the Aβ42 strain compared to Aβ40. These unique angle configurations result in the peptide planes in the fibril structures to be more vertical along the fibril axis for Aβ42 which thus reduces the inter-atomic distance between interacting atoms on vicinal peptide chains thereby increasing the electrostatic interaction energies. We lastly postulate that these different Ramachandran angle values could possibly be traced to the unique conformational folding avenues sampled by the Aβ42 peptide owing to the presence of its two extra residues.

Original languageEnglish (US)
Article number36499
JournalScientific reports
Volume6
DOIs
StatePublished - Nov 3 2016

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Amyloid
Peptides
Static Electricity
Alzheimer Disease
Pathology
peptide A42

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Few Ramachandran Angle Changes Provide Interaction Strength Increase in Aβ42 versus Aβ40 Amyloid Fibrils. / Bastidas, Oscar H.; Green, Benjamin; Sprague, Mary; Peters, Michael H.

In: Scientific reports, Vol. 6, 36499, 03.11.2016.

Research output: Contribution to journalArticle

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