Jump to main content
Jump to site search


Boc-Val-Val-OMe (Aβ39–40) and Boc-Ile-Ala-OMe (Aβ41–42) crystallize in a parallel β-sheet arrangement but generate a different morphology

Author affiliations

Abstract

Both N- and C-protected dipeptides, Boc-Val-Val-OMe (1) and Boc-Ile-Ala-OMe (2), bearing sequence homogeneity with the C-terminus of Alzheimer's Aβ39–40 and Aβ41–42, respectively, exhibit intermolecular hydrogen-bonded supramolecular parallel β-sheet structures in crystalline form. But the higher order aggregation of 2 showed a clear supramolecular cross-β-sheet structure unlike that of 1. FESEM images indicated that, while 1 self-assembled into a highly organized two ended spear-like architecture, 2 formed a hollow hexagonal tube-like structure, in a methanol–water solvent mixture. These molecules self-assembled into the ordered structures which found to bind with the amyloid binding dyes thioflavin T (ThT) and Congo red. FT-IR and PXRD also support the formation of the β-sheet structure both in solution and in the solid state. These results may help in understanding amyloidogenesis and design principle of nanostructures.

Graphical abstract: Boc-Val-Val-OMe (Aβ39–40) and Boc-Ile-Ala-OMe (Aβ41–42) crystallize in a parallel β-sheet arrangement but generate a different morphology

Back to tab navigation

Supplementary files

Publication details

The article was received on 22 Jan 2018, accepted on 28 Jun 2018 and first published on 29 Jun 2018


Article type: Paper
DOI: 10.1039/C8CE00097B
Citation: CrystEngComm, 2018, Advance Article
  •   Request permissions

    Boc-Val-Val-OMe (Aβ39–40) and Boc-Ile-Ala-OMe (Aβ41–42) crystallize in a parallel β-sheet arrangement but generate a different morphology

    R. S. Giri and B. Mandal, CrystEngComm, 2018, Advance Article , DOI: 10.1039/C8CE00097B

Search articles by author

Spotlight

Advertisements