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Macromolecular Crowding
Published in Mihai V. Putz, New Frontiers in Nanochemistry, 2020
Adriana Isvoran, Laura Pitulice, Eudald Vilaseca, Isabel Pastor, Sergio Madurga, Francesc Mas
Protein folding, stability, and association processes have been studied for many years in the diluted solution, but the effects of the cytosolic environment on these processes have only been considered for a few decades. The crowding agents do not bind covalently to the protein, but they change the properties of the environment of the protein. As protein misfolding and/or aggregation have been associated with several neurodegenerative diseases (Apetri and Surewicz, 2002; Winklhofer et al., 2008), it becomes important to study the protein’s behavior in their natural environment and take into consideration the effects of the environment.
Environmental Pollution: Increasing Risk of Neurodegenerative Diseases
Published in Hasnain Nangyal, Muhammad Saleem Khan, Environmental Pollution, Biodiversity, and Sustainable Development, 2020
Advancing loss of neuronal tissues in the central nervous system results in neurodegenerative disorders. Neurons start functioning abnormally and then decease gradually, as they lack the ability to regenerate on their own (Agrawal and Biswas, 2015). Several different factors contribute to the predisposition and precipitation of neurodegenerative disorders. This may also involve interaction between genetic predisposition and environmental factors. As a result of industrialization and bad waste management strategies, people are becoming more exposed to the toxic effects of environmental pollutants. Globally, neurodegenerative disorders are becoming a major threat to mental health with more cases reported each year. Between 1990 and 2010, neurological, mental, and substance abuse disorders were increased by 41% (Patel et al., 2016). Protein misfolding and aggregation use to be the underlying cause for neurodegenerative diseases, such as Parkinson’s, prion diseases, and others (Bose and Cho, 2016). Inhaled nanosized particles in the airborne particulate matter have been linked to several health effects including oxidative stress (OS) and neuroinflammation that may ultimately result in neurodegeneration and cognitive impairment (Heusinkveld et al., 2016). Heavy metal ions or other inhaled pollutants could precipitate neurodegenerative disorders by triggering protein misfolding (Tamás et al., 2014). Mitochondrial dysfunction, OS, and impaired enzymatic activities could be the resultant of excessive metal accumulation toxicity in the CNS (Farina et al., 2013). Environmental pollutants (serving as environmental cues) affect mental and physical wellness in the elderly as epigenetics suggests that environmental factors affect genetic imprinting (Modgil et al., 2014). Pre/postnatal exposure to these environmental cues predisposes the individual to neurodegenerative disorders due to defective growth and development of the brain.
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
The protein misfolding or aggregates is often manifested in the form of disease. There are many pathways through which amyloids mediate its cytotoxic effects. In many cases, amyloids have been shown to perform physiological functions.[139] Also there are many protein aggregates which are pathological, but not amyloids.[140,141] Amyloidoses are defined as the deposition of fibrillar aggregates extracellularly as plaques (Alzheimer’s disease, AD) and intracellularly as inclusions[142] (Parkinson’s and Huntington disease). Amyloidoses can also be categorized as systemic and localized. In systemic amyloidoses, multiple organs are affected while localized protein deposits occur in organ or tissues where precursor protein is synthesized. As for example in Type-II diabetes, islet amyloid polypeptide deposits occur in pancreatic tissues.[142] The neurodegenerative diseases are the most common form of amyloidoses. Some of the amyloid-related human diseases are listed below in Table 3[142]