Bibin G Anand
SRM Institute of Science and Technology, Kattankulathur
Bibin G Anand is a Research Assistant Professor from the Department of Biotechnology at SRM Institute of Science and Technology. He earned his PhD from IIT Jodhpur, specializing in designing nanomaterials to tackle protein aggregation. After his PhD, he moved to the University of Alberta in Canada, where he worked on engineered nano-shells to target Alzheimer's disease in vitro and in viva. He has also successfully secured funding from SynAD to study the role of functional nanoparticles on AD progression. Subsequently, he joined Boston University, where he explored eukaryotic transcription initiation factors and their role in triggering integrated stress responses in neurodegenerative diseases. He has published-37 research articles to date. He works in the fields of amyloid biology, neurodegeneration, and molecular self-assembly and believes that the most significant impact can be achieved through a blend of fundamental and translational research approaches. Selected as Associate in 2023.
Session 2C - Lectures by Fellows and Associates
Somdatta Sinha, IISER, Mohali
Understanding the molecular mechanism underlying protein and metabolite cross-catalysis and coalescence using bio-physical approaches
Conversion of proteins from their native form into aggregates can lead to the formation of highly stable structures known as amyloid fibrils characterized by cross p structures. Proteins and peptides with persistent folds and well-defined structures are prone to amyloid formation under different conditions, such as mutations, post-translational modification, impaired cellular mechanisms, and disrupted homeostasis. Approximately 50 proteins and peptides are known to form toxic amyloid entities, contributing to various pathological complications, including non-cerebral amyloidosis (systemic or localized) and neurodegenerative disorders. Even metabolites like phenylalanine, tyrosine, etc., tend to form a beta sheet-like structure with biophysical and biochemical properties like amyloids. However, due to the structural polymorphism displayed by amyloid fibrils, the precise molecular mechanisms behind these debilitating diseases remain a topic of ongoing debate. Our research tries to emphasize the significance of primary nucleation and secondary nucleation in the context of protein and metabolite aggregation, as well as their coalescence and cross-catalytic interactions. The results highlight the critical role of optimized intermolecular arrangements driven by aromatic interactions in facilitating coalescence and cross-catalysis events. These insights offer valuable clues for a fundamental and mechanistic understanding of the diverse pathological complications associated with neurodegenerative diseases. Furthermore, they shed light on the complicated nature of disease mechanisms and their direct association with amyloid formation in relevant proteins and metabolites.