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Aggregates have a variety of sizes and other physicochemical characteristics, making them diverse. As a direct consequence of this, a single technique is not merely sufficient to adequately analyze all the properties of aggregate particles. The findings acquired with one approach are inextricably related to those procured with another since every technique measures a different prospect of the enormous characteristic of aggregates. Development in protein aggregation research is driven by numerous approaches, including the structural study of protein aggregation. Besides, using numerous biophysical studies, the structural properties of amyloid at the insoluble and solvable processes have been reviewed, however, further research on the intermediate stage of the aggregated proteins is still under consideration. Herein, a short description of protein aggregation’s structural analysis strategies using various biophysical techniques has been discussed. Using Fluorescence spectroscopy, FTIR, NMR, and CD, structural modifications during protein aggregation can be understood which will help in developing therapeutics for many diseases induced by protein aggregation. Thus, along with other multidisciplinary methods, the insights obtained using these strategies will advance our level of awareness of protein aggregation and misfolding and related therapeutics for neurodegenerative diseases as well.

Protein unfolding leading to aggregation and amyloid formation has been explained. Protein aggregation and misfolding leading to the neuro-degeneration is described. Prominent neurodegenerative diseases with their features, diagnosis, and treatment are briefly described. Clinical trials and drugs for the treatment of neurodegenerative diseases are defined.

Mitochondria are among the most important organelles in eukaryotic cells and have a distinctive structure composed of lipid-bilayer membranes [1]. A mitochondrion has a unique structure comprising four parts the outer mitochondrial membrane (OMM), the inter-membranous space (IMS), the inner mitochondrial membrane (IMM), and the matrix, with each part performing a specific role. The permeability of mitochondrial lipid membranes differs; the outer membrane is permeable to a broad range of small molecules, but the inner membrane is selective [2]. The passage of molecules through the IMM is controlled by a variety of specialized channel proteins [3].

Mitochondria are among the most important organelles in eukaryotic cells and have a distinctive structure composed of lipid-bilayer membranes [1]. A mitochondrion has a unique structure comprising four parts the outer mitochondrial membrane (OMM), the inter-membranous space (IMS), the inner mitochondrial membrane (IMM), and the matrix, with each part performing a specific role. The permeability of mitochondrial lipid membranes differs; the outer membrane is permeable to a broad range of small molecules, but the inner membrane is selective [2]. The passage of molecules through the IMM is controlled by a variety of specialized channel proteins [3].