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Analysis of Natural and Engineered Amyloid Aggregates by Spectroscopic and Scattering Techniques

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Soft Matter Systems for Biomedical Applications

Part of the book series: Springer Proceedings in Physics ((SPPHY,volume 266))

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Abstract

The increasing knowledge about natural functional fibrils has triggered the interest in synthetic or engineered fibrils. Naturally occurring amyloid fibrils (functional and pathogenic) have been analyzed for many years at different structural levels. Engineered fibrils are structurally similar to natural fibrils and the main sub-structural feature of amyloids is characterized by cross-beta structure stabilizing the fibril formation. However, a number of peculiarities exist comparing natural and engineered fibrils that may affect their analysis, especially in spectroscopic and scattering methods. For this reason, several methods that are commonly used for natural fibril analysis are presented and particularities for their application in the characterization of engineered fibrils are described. In addition, the understanding about structure–function relation of fibrils studied in the different research areas may mutually improve when using the same analytical approaches for natural and engineered fibrils.

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Abbreviations

AFM:

Atomic force microscopy

ATR:

Attenuated total reflection

COSMiCS:

Complex objective structural analysis of multi component system

CW EPR:

Continuous wave EPR

DEER:

Double electron–electron resonance

DLS:

Dynamic light scattering

EPR:

Electron paramagnetic resonance

FTIR:

Fourier-transform infrared

SAXS:

Small angle X-ray scattering

SANS:

Small angle neutron scattering

SEM:

Scanning electron microscopy

SDSL:

Site directed spin labelling

ssNMR:

Solid state nuclear magnetic resonance

TEM:

Transmission electron microscopy

Thio-T:

Thioflavin-T

WAXS:

Wide angle X-ray scattering

Rg:

Radius of gyration

α-B-Cry:

α-B-crystallin

BLG:

Whey protein beta-lactoglobulin

BSA:

Bovine serum albumin

EGCG:

Epigallocatechin gallate

IPSL:

N-(1-oxyl-2,2,5,5-tetramethyl-3-pyrrolidinyl) iodoacetamide

MTSSL:

(1-Oxyl-2,2,5,5-tetramethylpyrroline-3-methyl) methanethiosulfonate

PGG:

Pentagalloyl glucose

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Acknowledgements

TRH, ASH, KS and JKK would like to thank the German Research Foundation (DFG), project number 315456892, within the priority program SPP1934.

Author information

Authors and Affiliations

  1. Institute of Human Nutrition and Food Science, Division of Food Technology, Kiel University, Kiel, Germany

    T. R. Heyn, Anja Steffen-Heins & K. Schwarz

  2. Helmholtz-Zentrum Hereon, Geesthacht, Germany

    V. M. Garamus

  3. Food Process Engineering Laboratory, Agrotechnology and Food Sciences Group, Wageningen University, Wageningen, The Netherlands

    J. K. Keppler

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  1. T. R. Heyn
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  2. V. M. Garamus
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  3. Anja Steffen-Heins
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  4. K. Schwarz
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  5. J. K. Keppler
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Corresponding author

Correspondence to V. M. Garamus .

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Editors and Affiliations

  1. Taras Shevchenko National University of Kyiv, Kyiv, Ukraine

    Leonid Bulavin

  2. National Academy of Science of Ukraine, Biocolloidal Chemistry Institute named after F.D. Ovharenko, Kyiv, Ukraine

    Nikolai Lebovka

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Heyn, T.R., Garamus, V.M., Steffen-Heins, A., Schwarz, K., Keppler, J.K. (2022). Analysis of Natural and Engineered Amyloid Aggregates by Spectroscopic and Scattering Techniques. In: Bulavin, L., Lebovka, N. (eds) Soft Matter Systems for Biomedical Applications. Springer Proceedings in Physics, vol 266. Springer, Cham. https://doi.org/10.1007/978-3-030-80924-9_11

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