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Nanotechnological Interventions for Neurodegenerative Disorders Using Phytoactives
Published in Bhupinder Singh, Om Prakash Katare, Eliana B. Souto, NanoAgroceuticals & NanoPhytoChemicals, 2018
Sumant Saini, Charan Singh, Shikha Lohan, Atul Jain, Eliana B. Souto, Bhupinder Singh
Protein aggregation has been considered an important cause of neurodegeneration. Accumulation of the misfolded proteins—such as α-synuclein (in PD) and β-amyloid (in AD)—is reported to be elevated in the clinical conditions of neurodegeneration. Recent studies have emphasized that there are common molecular and cellular mechanisms that govern neurodegenerative cascades. There has been increasing evidence suggesting that there is an accumulation of the truncated proteins in patients with neurodegenerative disorders. Such insights can pave the way towards novel therapeutic strategies for effective management of neurodegenerative disorders (Jucker and Walker, 2013).
Structure and interaction of therapeutic proteins in solution: a combined simulation and experimental study
Published in Molecular Physics, 2023
Suman Saurabh, Zongyi Li, Peter Hollowell, Thomas Waigh, Peixun Li, John Webster, John M. Seddon, Cavan Kalonia, Jian R. Lu, Fernando Bresme
Proteins are believed to aggregate through short-range interactions between hydrophobic and uncharged or charged regions of partially unfolded proteins. Quantifying the interaction between folded proteins as a function of distance can provide microscopic insight into the aggregation mechanism and help identify residues and regions which could potentially be modified to reduce aggregation. Specifically, protein aggregation takes place when aggregation-prone regions on the protein surface interact with each other. In solution, proteins undergo intermittent unfolding at the secondary and tertiary structure level, resulting in either transient or irreversible exposure of the aggregation hot spots at the protein surface. Undistorted proteins also form small reversible oligomeric clusters, which may precede subsequent unfolding of the protein, followed by aggregation [4–6].
Exploration of ligand-induced protein conformational alteration, aggregate formation, and its inhibition: A biophysical insight
Published in Preparative Biochemistry and Biotechnology, 2018
Saima Nusrat, Rizwan Hasan Khan
Protein aggregation is a highly dynamic process that represents the most remarkable consequence of protein misfolding and takes place in parallel with, or as an alternative to, physiological folding. Aggregation of proteins occurs in almost every stage of development, few research proposed that the non-native structures of protein are very prone to undergo aggregation.[83,84] Protein aggregates are categorized as: