About
21
Publications
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Introduction
Subrata Mondal currently works at the Department of Chemistry, Indian Institute of Technology Guwahati. Subrata does research in protein misfolding disease and their therapeutic strategy.
Current institution
Additional affiliations
March 2021 - present
April 2014 - July 2014
July 2015 - May 2021
Education
July 2013 - July 2015
August 2010 - May 2013
Publications
Publications (21)
Understanding molecular motifs that can interfere with amyloid fibrillation through non-covalent
interactions is essential for addressing abnormal protein aggregation and associated human diseases.
The pursuit of efficient diagnostic and treatment approaches for Alzheimer’s disease (AD) has resulted in
the development of M8HQ, a multifaceted small...
The emergence of neurodegenerative diseases is connected to several pathogenic factors, including metal ions, amyloidogenic proteins, and reactive oxygen species. Recent studies suggest that cytotoxicity is caused by the small, dynamic, and metastable nature of early stage oligomeric species. This work introduces a small molecule-based red-emitting...
Proteins, also known as polypeptides, comprise amino acid residues connected by peptide bonds and are one of the major biological macromolecules that play critical roles in every structure and activity of life. Therefore, it is crucial to identify the peptide molecules and purify them properly to understand their characteristics and functionality....
Point-of-care (PoC) diagnosis enables healthcare professionals to accurately perform lab-quality diagnostic test in real time within minutes rather than hours. It ensures patient to receive most effective and efficient care and health professional to track patient status or treatment response in real time. Hence, the advent of PoC devices has achie...
The robust and controllable sensitivity of thin film material and the outstanding stability of thin film make it an ideal choice for sensing applications. Analytes detected and analyzed ranging from detrimental gas molecules to biomolecules (nucleic acids, proteins) and diseases related biomarkers. This chapter outlines the working principle of che...
Alzheimer's Disease (AD) is an irreversible memory disorder associated with multiple neuropathological events includ-ing amyloid aggregation that triggers oxidative stress and mitochondrial dysfunction in humans. Herein, a new artificial chaperone PFBZ is reported to efficiently sequester toxic amyloid beta (Aβ) by binding at their 'Amyloidogenic d...
Intracellular calcium plays an important role in controlling cellular activities. A fluctuation of intracellular calcium level occurs continuously in the living cells due to the function of different physiological activities. Calcium is a signaling molecule. Different calcium regulating channels are present on the plasma membrane and the virus uses...
Nanoparticles have a wide applicability in the field of neuroscience in controlling different neurodegenerative disorders like Alzheimer’s disease, Parkinson’s disease, etc. These neurodegenerative disorders create a major health problem in the health care management. In most of the neurodegenerative disorders, hyper-excitability of neurons and sup...
The growth of smart wearable sensing systems has gained immense importance in the present mode of data acquisition and signaling in pharmaceutical, healthcare, and wellness industries. Presently, application of smart wearables is gaining prominence in several fitness activities, therapeutics, and diagnostic areas. Smart wearable biosensors offer re...
Polyvinylpyrrolidone (PVP)-based Silver nanoprisms (AgNPrs) show an initial stacking geometry due to their low zeta potential and electrostatic interaction between face-to-face energetically stable {111} surface-bound pyrrolidone groups through Na+ ion induced cation- interaction. Congested interplanner space between AgNPrs allows As(III) to react...
Low molecular weight (LMW) soluble amyloid oligomers have been established as primary neurotoxic species that play a key role in Alzheimer’s disease etiology. However, detection and separation of such energetically unfavored, metastable species are extremely challenging due to their short lifetime and dynamic nature. In this work, the aggregation o...
Molecular motifs that could interfere with amyloid fibrillation via non covalent interactions are very vital towards aberrant protein aggregation and related human diseases. Mutual aggregation ensues in the presence of these structural motifs and nucleation on the particle surface leads to inhibition of the fibrillization process. This modular proc...
Amyloid oligomers have emerged as a key neurotoxin in Alzheimer’s dementia. Amyloid aggregation inhibitors and modulators have therefore offered potential applications in therapeutics and diagnosis. However, crossing the blood–brain barrier (BBB) and finding the toxic aggregates among aggregates of different sizes and shapes remain a challenge. The...
Amyloid aggregation is observed in many neurodegenerative diseases but the formation of final plaque seldom correlates to the disease severity. Early and intermediate structures such as soluble oligomers are considered as primary toxic species in protein misfolding diseases specifically linked to Aβ in Alzheimer’s disease (AD). Two peptides linked...
Amyloid aggregation is most important pathological hallmarks toward
Alzheimer’s disease.
• GNP-NMDA inhibits amyloid aggregation in commercial Aβ1-40 and as
well as in human CSF sample.
•This plasmonic NP forms an electrical double layer with toxic amyloid
oligomers and disturbs their self-aggregation toward plaque formation as
found in the disease...
Amyloid aggregation is one of the most important pathological hallmarks toward Alzheimer's disease. • Polyfluorene-chitosan (PC) composite inhibits amyloid aggregation in commercial Aβ1-40 and as well as in human CSF sample. •This polymeric composite mask the toxic amyloid oligomers to come close to each other and disturbs their self-aggregation to...
Questions
Question (1)
Amyloid aggregation is a multistep process in which nucleation is the obligatory step. Many thermodynamic factor contribute to the aggregation kinetics. What is the role of entropy and enthalpy in the amyloid aggregation?