Osmolytes and Intrinsically Disordered Proteins: From Functional Regulation to Disease Pathogenesis

Dr. Tanveer Ali Dar, affiliated with University of Kashmir, stands as a pioneer in the dynamic and evolving field of osmolyte-protein biology. Holding advanced degrees in his field, Dr. Dar has dedicated his career to advancing scientific knowledge and innovation in osmolyte research. Utilizing a multidisciplinary approach that combines biochemical, biophysical, and molecular biology techniques, Dr. Dar explores the dynamic interplay between osmolytes and proteins at the molecular level. His research sheds light on how osmolytes modulate protein structure and dynamics, enabling cells to adapt and thrive under stressful conditions such as osmotic stress, temperature fluctuations, and disease states. He has to his credit several breakthrough contributions in the area of exploring the osmolyte induced structural-functional integrity of proteins and their implications in protein misfolding disease interventions. Besides focusing on several aspects of osmolyte research, his research particularly emphasizes on understanding the roles of osmolytes and intrinsically disordered proteins in cellular function and disease pathogenesis. His pioneering investigations have shed light on the dynamic interplay between these molecular entities, unraveling fundamental mechanisms underlying cellular resilience and disease progression. Dr. Dar is recognized for his contributions to both theoretical understanding and practical applications in the osmolyte-field, and his work has been published in numerous peer-reviewed international journals. Moreover, he has to his credit a couple of books published by Springer International Ltd., Apple academic Press and Elsevier, USA. Dr. Dar is also a recipient of Indian National Science Academy visiting fellowship and is a member of various international and national scientific societies like ASBMB, Canadian Society of Molecular Biosciences, National Academy of Sciences India, India Biophysical society etc. He is a prolific reviewer, editor and editorial board member of a number of prestigious journals. As an educator, he is committed to nurturing the next generation of scientists, mentoring students and guiding them towards excellence in research. Prof. Laishram R. Singh is a pioneer in the field of osmolyte research. He has made several landmark contributions in understanding protein folding mechanism by osmolytes and harnessing the basic knowledge in designing strategies for the therapeutic intervention of human diseases caused by protein folding defects. He obtained his doctoral degree (in the year 2006) from Jamia Millia Islamia, New Delhi from where he begins his research on osmoprotectants, unveiling their role in protein folding landscape and thermodynamics of protein folding. He then expanded his expertise during his postdoctoral studies at Fox Chase Cancer Cancer, Philadelphia by employing these molecules for restoring functions to disease causing mutant proteins related to homocystinuria. Nowadays, metabolomic studies has further expanded the repertoire of osmolytic molecules that are upregulated or downregulated under various disease conditions including neurodegenerative diseases. Presently, at the University of Delhi, he is engaged on identifying specific brain osmolytes that could regulate the functional activity of acetylcholinesterase and carbonic anhydrase (important target enzymes of Dementia). He is also interested in using these osmolytes to correct folding defects of some of the folding deficient brain proteins including, Aß, a-synuclein, transthyretin whose toxic inclusions are the emblematic signatures of Dementia. He has published more than 85 articles related to the avenue “osmolyte research” in various journals of high international repute. He is a prolific reviewer, guest editors, and is in the editorial board members of prestigious journals. Prof. Vladimir N. Uversky, PhD, DSc, FRSB, FRSC, F.A.I.M.B.E., Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida (USF), is a pioneer in the field of protein intrinsic disorder. He has made a number of groundbreaking contributions in the field of protein folding, misfolding, and intrinsic disorder. He obtained his academic degrees from Moscow Institute of Physics and Technology (Ph.D., in 1991) and from the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences (D.Sc., in 1998). He spent his early career working mostly on protein folding at the Institute of Protein Research and the Institute for Biological Instrumentation (Russia). In 1998, moved to the University of California Santa Cruz. In 2004, joined the Indiana University−Purdue University Indianapolis as a Senior Research Professor. Since 2010, Professor Uversky is with USF, where he works on various aspects of protein intrinsic disorder phenomenon and on analysis of protein folding and misfolding processes. Prof. Uversky has authored over 1250 scientific publications and edited several books and book series on protein structure, function, folding, misfolding, and intrinsic disorder. He is also serving as an editor in a number of scientific journals. He was a co-founder of the Intrinsically Disordered Proteins Subgroup at the Biophysical Society and the Intrinsically Disordered Proteins Gordon Research Conference. Prof. Uversky collaborated with more than 12,500 colleagues from more than 2,750 research organizations in 89 countries/territories.

1. Functional diversity of IDPs and their structural heterogeneity: Protein structure-function continuum
Vladimir N. Uversky
2. Osmolytes as structure-function regulators of intrinsically disordered casein
Mohd. Younus Bhat
3. Synergism of the effects of osmolytes and crowders on structure and function of IDPs/IDRs: The natural habitat
Terrence G. Oas
4. Osmolyte-IDP Interactions during Desiccation
Vincent Nicholson, Thomas Boothby and Emma K. Meese
5. Modulation of aggregation/fibrillation propensity of IDPs by osmolytes
Tanveer Ali Dar Sr.
6. Osmolytes in modulating the structural and functional integrity of a-synuclein: a study based on Parkinson's disease
Laishram R. Singh
7. Regulation of the structural dynamics, aggregation, and pathogenicity of polyQ-expanded Huntingtin by osmolytes.
Alice Y. Liu, Amala Mathew, Christopher Karim, Pierre Eshak and Kuang Yu Chen
8. Md Nadir Hassan, Murtaza Hussain, Rizwan Hasan Khan, Aggregation and inhibitory strategies of amyloid fibrillation
Rizwan Hasan Khan and Rizwan H. Khan
9. Modulation of amyloid beta and Tau aggregation by Phytochemicals: Implications in Alzheimer’s Disease
Mohd. Kamil Hussain, Shakir Ahamad, Moazzam Ahmad, Mohammad Saquib, Shahnaaz Khatoon, Karam Fatima and Mohsin Vahid Khan
10. The Emerging Landscape of Natural Small-molecule Therapeutics for Huntington’s Disease
Shahnawaz Ali Bhat, Shakir Ahamad, Sameera Khan and Nargis Bano
11. Molecular crowding and amyloidogenic self-assembly: emergent perspectives from modern computations
Neelanjana Sengupta