Single molecule biophysics Lab

Study of Protein Amyloids and Liquid-liquid Phase Separation (LLPS) using Single Molecule Techniques: Aggregation of amyloidogenic proteins are associated in the pathology of multiple human diseases, such as Alzheimer’s and Parkinson’s disease and Type 2 diabetes. The main goal of our research to investigate the molecular mechanisms of its aggregation. Endogenous proteins such as chaperones and apolipoprotein E are known the influence the progression of the above-mentioned diseases. We are using an array of biophysical techniques to investigate the role of these proteins on protein aggregation.

Amyloid beta peptide (Aβ): Aggregation and deposition of Aβ in the brain is hallmark of Alzheimer’s disease.

Alpha-synuclein: Primary component of the Lewy bodies and Lewy neurites in Parkinson disease and other synucleinopathies.

Tau protein: Tau is the major microtubule associated protein (MAP) in neurons. Aberrant aggregation of tau is involved in the pathology of Alzheimer’s disease and other tauopathies.

Islet amyloid polypeptide (IAPP) or Amylin: A 37 -residue peptide hormone, which plays important roles in glycaemic regulation. Aggregation of IAPP inside the pancreatic islets is involved in the pathology of Type 2 diabetes mellitus (T2DM).

LLPS: Many intrinsically disordered proteins (IDPs) undergo LLPS separating into protein dilute and protein rich phases. These LLPS subsequently mature to gel-like solids or to amyloid fibrils. We study the physicochemical properties of the LLPS of several IDPS including amyloid, alpha-synuclein and tau.

Single Molecule Techniques: We build and use various single molecule spectroscopy and imaging techniques to study protein amyloids and LLPS droplets. The techniques built in the lab are Fluorescence Correlation Spectroscopy (FCS), Cuvette-FCS, single molecule FRET (smFRET), Two-Color Coincidence Detection (TCCD), Total Internal Reflection Fluorescence Microscopy (TIRFM), Superresolution Optical Microscopy etc.