This study provides a platform for trehalose in the therapeutic management of protein aggregation-related diseases
2021
Trehalose Restrains the Fibril Load towards α-Lactalbumin Aggregation and Halts Fibrillation in a Concentration-Dependent Manner
Key concepts
Scholarcy highlights
- Several neurodegenerative diseases leading to amyloid fibrils and plaques are unambiguously associated with the intracellular aggregation of proteins
- Maximum reduction was observed for 1 M trehalose. These observations were in line with earlier results that implied that the presence of 1 M trehalose prevented the aggregation of α-LA maximally; i.e., it acted as the best inhibitor in preventing the aggregation of α-LA
- UV-Vis spectroscopy, a Thioflavin T binding assay, intrinsic fluorescence, Rayleigh scattering and turbidity assay measurements showed that the presence of trehalose inhibited α-LA
- Aggregation in a dosage-dependent manner with 1 M trehalose acting as the best concentration causing the maximal inhibition of protein aggregation. Microscopic techniques complemented these observations; TEM analysis suggested that the native α-LA was transformed into fibrils when subjected to thermal treatment and 1 M trehalose inhibited aggregation in αLA
- Molecular docking studies suggested that trehalose as a potent binding partner of α-LA and hydrogen bonding were the key players in this interaction
- Together with spectroscopic and microscopic observations, these observations affirmed that trehalose bonded with α-LA and the presence of 1 M trehalose prevented the aggregation of α-LA
- This research gives evidence of the benefits of the naturally occurring sugars as inhibitors of amyloid fibril production and the possible use of naturally occurring sugar osmolytes for the therapeutic management of protein aggregation-related disorders
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