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Lipids in Protein Misfolding pp 33–66Cite as

Protein Misfolding in Lipid-Mimetic Environments

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 855))

Abstract

Among various cellular factors contributing to protein misfolding and subsequent aggregation, membranes occupy a special position due to the two-way relations between the aggregating proteins and cell membranes. On one hand, the unstable, toxic pre-fibrillar aggregates may interact with cell membranes, impairing their functions, altering ion distribution across the membranes, and possibly forming non-specific membrane pores. On the other hand, membranes, too, can modify structures of many proteins and affect the misfolding and aggregation of amyloidogenic proteins. The effects of membranes on protein structure and aggregation can be described in terms of the “membrane field” that takes into account both the negative electrostatic potential of the membrane surface and the local decrease in the dielectric constant. Water-alcohol (or other organic solvent) mixtures at moderately low pH are used as model systems to study the joint action of the local decrease of pH and dielectric constant near the membrane surface on the structure and aggregation of proteins. This chapter describes general mechanisms of structural changes of proteins in such model environments and provides examples of various proteins aggregating in the “membrane field” or in lipid-mimetic environments.

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Abbreviations

Aβ:

Amyloid-β

AFM:

Atomic force microscopy

ANS:

Anilino-8-napthalene sulfonate

CD:

Circular dichroism

DMPC:

Dimyristoyl phosphatidylcholine

DMPG:

1,2-dimyristoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] sodium salt

DMPS:

Dimyristoyl phosphatidylserine

EtOH:

Ethanol

FTIR:

Fourier transform infrared spectroscopy

HFiP:

1,1,1,3,3,3-hexafluoro-2-propanol

HSA:

Human serum albumin

IAPP:

Islet amyloid polypeptide

IDP:

Intrinsically disordered protein

IDPR:

Intrinsically disordered protein region

LUV:

Large unilamellar vesicle

MeOH:

Methanol

nFGF-1:

Newt acidic fibroblast growth factor

PA:

1,2-dipalmitoyl-sn-glycero-3-phosphate

PC:

1,2-dipalmitoyl-sn-glycero-3-phospho-choline

PE:

1-palmitoyl-2-oleoyl-phosphoethano-lamine

PG:

1,2- dipalmitoyl-sn-glycero-3-phospho-RAC-(1-glycerol)

PI:

Phosphatidylinositol

PrOH:

Propanol

PS:

1-palmitoyl-2-oleoyl-phosphatidylserine

SUV:

Small unilamellar vesicle

TFE:

2,2,2-trifluoroethanol

ThT:

Thioflavin T

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Acknowledgements

This work was supported in part by a grant from Russian Science Foundation RSCF № 14-24-00131

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Authors and Affiliations

  1. Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd. MDC07, Tampa, FL, 33612, USA

    Vladimir N. Uversky

  2. Biology Department, Faculty of Science, King Abdulaziz University, 80203, Jeddah, 21589, Kingdom of Saudi Arabia

    Vladimir N. Uversky

  3. Institute for Biological Instrumentation, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russia

    Vladimir N. Uversky

  4. Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia

    Vladimir N. Uversky

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  1. Vladimir N. Uversky
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Correspondence to Vladimir N. Uversky .

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  1. Dept. of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts, USA

    Olga Gursky

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Uversky, V.N. (2015). Protein Misfolding in Lipid-Mimetic Environments. In: Gursky, O. (eds) Lipids in Protein Misfolding. Advances in Experimental Medicine and Biology, vol 855. Springer, Cham. https://doi.org/10.1007/978-3-319-17344-3_2

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