Sequence-Dependent Self-Assembly and Structural Diversity of Islet Amyloid Polypeptide-Derived β-Sheet Fibrils

Wang, Shih-Ting; Lin, Yiyang; Spencer, Ryan K.; Thomas, Michael R.; Nguyen, Andy I.; Amdursky, Nadav; Pashuck, E. Thomas; Skaalure, Stacey C.; Song, Cheng Yu; Parmar, Paresh A.; Morgan, Rhodri M.; Ercius, Peter; Aloni, Shaul; Zuckermann, Ronald N.; Stevens, Molly M.

doi:10.1021/acsnano.7b02325

Title: Sequence-Dependent Self-Assembly and Structural Diversity of Islet Amyloid Polypeptide-Derived β-Sheet Fibrils

Journal Article · Thu Aug 03 00:00:00 EDT 2017 · ACS Nano

DOI:https://doi.org/10.1021/acsnano.7b02325· OSTI ID:1416928

Wang, Shih-Ting ^[1]; Lin, Yiyang ^[1]; Spencer, Ryan K. ^[2];

^[1];

^[2]; Amdursky, Nadav ^[1];

^[1]; Skaalure, Stacey C. ^[1]; Song, Cheng Yu ^[2]; Parmar, Paresh A. ^[1]; Morgan, Rhodri M. ^[3]; Ercius, Peter ^[2]; Aloni, Shaul ^[2];

^[2];

^[1]

Imperial College, London (United Kingdom). Inst. of Biomedical Engineering, Dept. of Materials and Dept. of Bioengineering
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Foundry
Imperial College, London (United Kingdom). Dept. of Life Sciences

Determining the structural origins of amyloid fibrillation is essential for understanding both the pathology of amyloidosis and the rational design of inhibitors to prevent or reverse amyloid formation. In this work, the decisive roles of peptide structures on amyloid self-assembly and morphological diversity were investigated by the design of eight amyloidogenic peptides derived from islet amyloid polypeptide. Among the segments, two distinct morphologies were highlighted in the form of twisted and planar (untwisted) ribbons with varied diameters, thicknesses, and lengths. In particular, transformation of amyloid fibrils from twisted ribbons into untwisted structures was triggered by substitution of the C-terminal serine with threonine, where the side chain methyl group was responsible for the distinct morphological change. This effect was confirmed following serine substitution with alanine and valine and was ascribed to the restriction of intersheet torsional strain through the increased hydrophobic interactions and hydrogen bonding. We also studied the variation of fibril morphology (i.e., association and helicity) and peptide aggregation propensity by increasing the hydrophobicity of the peptide side group, capping the N-terminus, and extending sequence length. Lastly, we anticipate that our insights into sequence-dependent fibrillation and morphological diversity will shed light on the structural interpretation of amyloidogenesis and development of structure-specific imaging agents and aggregation inhibitors.

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Research Organization:: Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); Taiwan Strategic Alliance; Engineering and Physical Sciences Research Council (EPSRC)

Grant/Contract Number:: AC02-05CH11231; EP/K020641/1

OSTI ID:: 1416928

Journal Information:: ACS Nano, Vol. 11, Issue 9; ISSN 1936-0851

Publisher:: American Chemical Society (ACS)Copyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 35 works

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37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
amyloid fibrils
helical nanostructures
islet amyloid polypeptide
nanoribbons
self-assembly

Title: Sequence-Dependent Self-Assembly and Structural Diversity of Islet Amyloid Polypeptide-Derived β-Sheet Fibrils

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