Abstract
Amyloid diseases are of major concern all over the world due to a number of factors including: (i) aging population, (ii) increasing life span and (iii) lack of effective pharmacotherapy options. The past decade has seen intense research in discovering disease-modifying multi-targeting small molecules as therapeutic options. In recent years, targeting the amyloid cascade has emerged as an attractive strategy to discover novel neurotherapeutics. Formation of amyloid species, with different degrees of solubility and neurotoxicity is associated with the gradual decline in cognition leading to dementia/cell dysfunction. Here, in this chapter, we have described the recent scenario of amyloid diseases with a great deal of information about the structural features of oligomers, protofibrils and fibrils. Also, comprehensive details have been provided to differentiate the degree of toxicity associated with prefibrillar aggregates. Moreover, a review of the technologies that aid characterisation of oligomer, protofibrils and fibrils as well as various inhibition strategies to overcome protein fibrillation are also discussed.
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Acknowledgements
Facilities provided by Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh are gratefully acknowledged. For providing financial assistance, M.K.S. is thankful to Department of Biotechnology (DBT), New Delhi, India, P.A. and N.M. are thankful to Council of Scientific and Industrial Research (CSIR), New Delhi, India, S.M. is thankful to Indian Council of Medical Research (ICMR), New Delhi, India. R.H.K. is thankful to CSIR and UGC for project referenced as 37(1676)/17/EMR—II and F. 19-219/2018, respectively.
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Siddiqi, M.K., Majid, N., Malik, S., Alam, P., Khan, R.H. (2019). Amyloid Oligomers, Protofibrils and Fibrils. In: Harris, J., Marles-Wright, J. (eds) Macromolecular Protein Complexes II: Structure and Function . Subcellular Biochemistry, vol 93. Springer, Cham. https://doi.org/10.1007/978-3-030-28151-9_16
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