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Evaluation of nanoparticle tracking for characterization of fibrillar protein aggregates
Author(s) -
Yang Dennis T.,
Lu Xiaomeng,
Fan Yamin,
Murphy Regina M.
Publication year - 2014
Publication title -
aiche journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.958
H-Index - 167
eISSN - 1547-5905
pISSN - 0001-1541
DOI - 10.1002/aic.14349
Subject(s) - transthyretin , hydrodynamic radius , nanoparticle tracking analysis , chemistry , characterization (materials science) , nanoparticle , diffusion , tracking (education) , amyloid fibril , fibril , protein aggregation , biophysics , particle (ecology) , amyloid disease , macromolecule , particle size , amyloid (mycology) , nanotechnology , materials science , biochemistry , amyloid β , microvesicles , physics , thermodynamics , biology , microrna , pedagogy , endocrinology , ecology , pathology , dynamic light scattering , psychology , inorganic chemistry , medicine , disease , gene
Amyloidogenesis is the process of formation of protein aggregates with fibrillar morphology. Because amyloidogenesis is linked to neurodegenerative disease, there is interest in understanding the mechanism of fibril growth. Kinetic models of amyloidogenesis require data on the number concentration and size distribution of aggregates, but this information is difficult to obtain using conventional methods. Nanoparticle tracking analysis (NTA) is a relatively new technique that may be uniquely suited for obtaining these data. In NTA, the two‐dimensional (2‐D) trajectory of individual particles is tracked, from which the diffusion coefficient, and, hence, hydrodynamic radius is obtained. Here we examine the validity of NTA in tracking number concentration and size of DNA, as a model of a fibrillar macromolecule. We use NTA to examine three amyloidogenic materials: beta‐amyloid, transthyretin, and polyglutamine‐containing peptides. Our results are instructive in demonstrating the advantages and some limitations of single‐particle diffusion measurements for investigating aggregation in protein systems. © 2014 American Institute of Chemical Engineers AIChE J , 60: 1236–1244, 2014