Subhadeep Das

Subhadeep Das
Indian Institute of Technology Bombay | IIT Bombay ·  Department of Biosciences & Bioengineering

PhD

About

25
Publications
5,229
Reads
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658
Citations
Additional affiliations
August 2011 - December 2011
Bose Institute
Position
  • Researcher
Education
January 2012 - January 2016
Indian Institute of Technology Bombay
Field of study
  • Bioengineering
August 2009 - May 2011
Madurai Kamaraj University
Field of study
  • Biotechnology
August 2006 - May 2009
University of Calcutta
Field of study
  • Biochemistry

Publications

Publications (25)
Article
Amyloid formation of α-synuclein (α-Syn) and its familial mutations are directly linked with Parkinson’s disease (PD) pathogenesis. Recently, a new familial α-Syn mutation (A53E) was discovered, associated with an early-onset aggressive form of PD, which delays the α-Syn aggregation. When we overexpressed WT and A53E proteins in cells, neither of t...
Article
Amyloid fibrils are cross-β-sheet rich protein/peptide fibrils that are typically associated with neurodegenerative diseases such as Parkinson’s and Alzheimer’s disease. Recently, functional amyloids have been discovered where amyloids are implicated in performing normal physiological functions of the host organism rather than creating diseases. Th...
Article
Full-text available
Parkinson's disease is a sporadic disorder in which both environmental and cellular factors play a major role in the initiation of this disease. Glycosaminoglycans (GAGs) are integral components of the extracellular matrix and are known to influence amyloid aggregation of several proteins, including α-synuclein (α-Syn). However, the mechanism by wh...
Article
Graphene‐based hybrid nanomaterials have been shown to have great potential in various biotechnology applications including enzyme sensing and bone tissue engineering. Harnessing the unique properties of graphene and material strength of amyloids, a graphene–amyloid composite film is developed that can self‐organize into periodic troughs and crests...
Article
Full-text available
α-Synuclein (α-Syn) aggregation and amyloid formation are associated with loss of dopaminergic neurons in Parkinson’s disease (PD). In addition, familial mutations in α-Syn are shown to be one of the definite causes of PD. Here we have extensively studied familial PD associated α-Syn G51D, H50Q and E46K mutations using Drosophila model system. Our...
Article
The involvement of α-synuclein (α-Syn) amyloid formation in Parkinson’s disease (PD) pathogenesis is supported by the discovery of α-Syn gene (SNCA) mutations linked with familial PD, which are known to modulate the oligomerization and aggregation of α-Syn. Recently, the A53V mutation has been discovered, which leads to the late-onset PD. In the pr...
Article
Extracellular matrices (ECM) play an enormous role in any living system, controlling various factors and eventually fates of cells. ECM regulates cell fate by providing constant exogenous signals altering intracellular signal transduction for diverse pathways including proliferation, migration, differentiation and apoptosis. Biomaterial scaffolds a...
Article
α-synuclein (α-Syn) aggregation is associated with Parkinson's disease (PD) pathogenesis. In PD, the role of oligomer versus fibrils in neuronal cell death is debatable but recent studies suggest oligomers are a proximate neurotoxin. Here, we show that soluble α-Syn monomers convert from solution to gel state on incubation at high concentration tha...
Article
Syn) aggregation is associated with Parkinson's disease (PD) pathogenesis. In PD, the role of oligomer versus fibrils in neuronal cell death is debatable but recent studies suggest oligomers are a proximate neurotoxin. Here, we show that soluble α-Syn monomers convert from solution to gel state on incubation at high concentration that might be rele...
Chapter
Amyloids are highly ordered peptide/protein aggregates traditionally associated with multiple human diseases including neurodegenerative disorders. However, recent studies suggest that amyloids can also perform several biological functions in organisms varying from bacteria to mammals. In many lower organisms, amyloid fibrils function as adhesives...
Article
Samir K. Maji and co-workers present an amyloid hydrogel for sustained growth factors delivery in tissue engineering applications in article number 1700368. The image represents stem cells (blue spheres) embedded within the amyloid hydrogel matrix (grey network) encapsulating growth factors (green dots). Within 3D culture, stem cells self-organizes...
Article
Full-text available
The master regulator, DnrI of Streptomyces peucetius is a member of the family of transcriptional activator, Streptomyces antibiotic regulatory proteins (SARP), which controls the biosynthesis of antitumor anthracycline, daunorubicin (DNR) and doxorubicin (DXR). The binding of DnrI to the heptameric repeat sequence found within the -35 promoter reg...
Article
Full-text available
Amyloid based hydrogels can mimic the extracellular matrix and serve as matrices for tissue engineering both in vitro and in vivo. A pH responsive self-assembled amyloid hydrogel system is used to encapsulate various growth factors for driving stem cell differentiation toward neuronal lineage. Diffusion studies with fluorescence recovery after phot...
Article
Full-text available
We report a new class of amyloid-inspired peptide hydrogels that was designed and based on α-synuclein protein for which hydrogel formation is triggered by various stimuli, such as heating/cooling or changes in pH. The peptides resemble a cross-β-sheet-rich amyloid, and they assemble into a nanofibrous meshwork that mimics the natural extracellular...
Article
Full-text available
Alpha-synuclein (α-Syn) aggregation into oligomers and fibrils is associated with dopaminergic neuron loss occurring in Parkinson’s disease (PD) pathogenesis. Compounds that modulate α-Syn aggregation and interact with preformed fibrils/oligomers and convert them to less toxic species could have promising applications in the drug development effort...
Article
Full-text available
Amyloids are cross-β-sheet fibrillar aggregates, associated with various human diseases and native functions such as protein/peptide hormone storage inside secretory granules of neuroendocrine cells. In the current study, using amyloid detecting agents, we show that growth hormone (GH) could be stored as amyloid in the pituitary of rat. Moreover, t...
Article
Full-text available
This paper presents data related to the research article “Self healing hydrogels composed of amyloid nano fibrils for cell culture and stem cell differentiation” [1]. Here we probed the collective influence of all-trans retinoic acid (RA) and substrate properties (amyloid hydrogel) on human mesenchymal stem cell (hMSC) differentiation. Stem cells w...
Article
Amyloids are highly ordered protein/peptide aggregates associated with human diseases as well as various native biological functions. Given the diverse range of physiochemical properties of amyloids, we hypothesized that higher order amyloid self-assembly could be used for fabricating novel hydrogels for biomaterial applications. For proof of conce...
Article
Amyloids are highly ordered protein/peptide aggregates associated with human diseases as well as various native biological functions. Given the diverse range of physiochemical properties of amyloids, we hypothesized that higher order amyloid self-assembly could be used for fabricating novel hydrogels for biomaterial applications. For proof of conce...
Article
Full-text available
The storage of protein/peptide hormones within sub-cellular compartments and subsequent release are crucial for their native function, and hence these processes are intricately regulated in mammalian systems. Several peptide hormones were recently suggested to be stored as amyloids within endocrine secretory granules. This leads to an apparent para...
Article
It has been suggested that conjugated charged polymers are amyloid imaging agents and promising therapeutic candidates for neurological disorders. However, very less is known about their efficacy in modulating the amyloid aggregation pathway. Here, we studied the modulation of Parkinson's disease associated α-synuclein (AS) amyloid assembly kinetic...

Questions

Question (1)
Question
I have observed very often that hMSCs cultured in standard TC flasks adhere more strongly if cultured for longer periods (say 3-4 weeks) without splitting. The initial seeding density is such that they do not overgrow in that time frame. This is reflected in increased trypsinisation time. Has anyone else observed the same/

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Projects

Projects (3)
Project
Currently iInvestigating the cues that mediate the formation and maturation of alpha-Synuclein liquid condensates.