Publication

Detection of protein aggregation with a Bloch surface wave based sensor

Hans Peter Herzig, Vincent Paeder, Lubos Hvozdara, Valeria Musi, Sylvain Herminjard
2011
Journal Articles

Abstract

We present the innovative application of a Bloch surface wave based sensor to the detection of protein aggregation. In Hen Egg White Lysozyme (HEWL) solutions, aggregates are discriminated from the monomeric forms in a label-free detection scheme.

Official source

https://infoscience.epfl.ch/entities/publication/e1442416-2b8a-4b9c-acb8-51c64075b82b

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Hans Peter Herzig, Vincent Paeder, Lubos Hvozdara, Valeria Musi, Sylvain Herminjard
2011
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/e1442416-2b8a-4b9c-acb8-51c64075b82b

About this result

Related concepts (6)

Protein aggregation

In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly. Protein aggregates have been implicated in a wide variety of diseases known as amyloidoses, including ALS, Alzheimer's, Parkinson's and prion disease. After synthesis, proteins typically fold into a particular three-dimensional conformation that is the most thermodynamically favorable: their native state.

Protein folding

Protein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.

Tau protein

The tau proteins (abbreviated from tubulin associated unit) are a group of six highly soluble protein isoforms produced by alternative splicing from the gene MAPT (microtubule-associated protein tau). They have roles primarily in maintaining the stability of microtubules in axons and are abundant in the neurons of the central nervous system (CNS), where the cerebral cortex has the highest abundance. They are less common elsewhere but are also expressed at very low levels in CNS astrocytes and oligodendrocytes.

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