Observation of two-step aggregation kinetics of amyloid-beta proteins from fractal analysis
Mukhopadhyay S, Bera SC, Ramola K (2022)
Publication Type: Journal article
Publication year: 2022
Journal
Book Volume: 19
Journal Issue: 4
Abstract
Self-aggregation in proteins has long been studied and modeled due to its ubiquity and importance in many biological contexts. Several models propose a two step aggregation mechanism, consisting of linear growth of fibrils and secondary growth involving branch formation. Single molecule imaging techniques such as total internal reflection fluorescence (TIRF) microscopy can provide direct evidence of such mechanisms, however, analyzing such large data-sets is challenging. In this paper, we analyze for the first time, images of growing amyloid fibrils obtained from TIRF microscopy using the techniques of fractal geometry, which provides a natural framework to disentangle the two types of growth mechanisms at play. We find that after an initial linear growth phase, identified by a plateau in the average fractal dimension with time, the occurrence of branching events leads to a further increase in the fractal dimension, with a final saturation value approximate to 2. This provides direct evidence of the two-step nature of the aggregation kinetics of amyloid-beta proteins, with an initial linear elongation phase followed by branching at later times.
Authors with CRIS profile
Subhas Chandra Bera
Interdisziplinäres Zentrum für Klinische Forschung IZKF Nachwuchsgruppe 2 Prof. Dr. Dulin
Involved external institutions
India (IN)How to cite
APA:
Mukhopadhyay, S., Bera, S.C., & Ramola, K. (2022). Observation of two-step aggregation kinetics of amyloid-beta proteins from fractal analysis. Physical Biology, 19(4). https://dx.doi.org/10.1088/1478-3975/ac6478
MLA:
Mukhopadhyay, Soham, Subhas Chandra Bera, and Kabir Ramola. "Observation of two-step aggregation kinetics of amyloid-beta proteins from fractal analysis." Physical Biology 19.4 (2022).
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