Cameron Students posing for a picture on Campus

Physical Chemistry

Physical Chemistry is the study of macroscopic, atomic, subatomic, and particulate phenomena in chemical systems in terms of the principles, practices, and concepts of physics such as motion, energy, force, time, thermodynamics, quantum chemistry, statistical mechanics, analytical dynamics and chemical equilibrium. 

Project 1: Photophysical Properties of Fluorescent Dyes Inside Reverse micelle:

The photo physical properties of Cyanine-5 (Cy5) and Texas Red dyes in aqueous and confined reverse-micellar environments have been investigated by using steady-state UV-Vis absorption and emission and time-resolved fluorescence spectroscopic techniques. For these studies, the fluorescent dye molecules were encapsulated in both anionic sodium-di-2ethylhexyl sulfosuccinate (AOT) reverse micelles and cationic cetyltrimethyl bromide (CTAB) reverse micelles of various sizes. The photo physical properties of the dyes in water as well as in reverse micelles of various sizes were examined by analyzing various photo physical parameters. Our observation shows that Cy 5 behaves very differently inside the reverse micelle as compared to the aqueous environment. Texas Red dyes behave very differently as compared to cyanine cy5 dyes. These are the very exciting results and have encouraged our research group to use these probe molecules to investigate the dynamic properties of the biomolecule in confined reverse micellar environment.


Project 2: Protein folding kinetics of Alzheimer peptide in confined environment: The accumulation of insoluble β-amyloid 

Plaques in the brain is one of the prominent reasons of Alzheimer’s Disease (AD).5 It is not clear whether this plaque formation is the cause of the disease. However, enough evidence suggests that the disease is initiated by the production, aggregation and deposition of the amyloid β-peptide (Aβ) in the brain.6 The amyloid β-peptide of 40 and 42 amino acid residues, commonly known as Aβ(1-40) and Aβ(1- 42) monomers, aggregate into insoluble clumps, responsible for synaptic dysfunction in the brains of AD patients. I propose to address these questions of protein folding kinetics using various steady-state and time-resolved spectroscopic techniques by encapsulating peptides into RMs of different sizes.