Research Interests

Carbon Dots

Carbon Dots were discovered at the beginning of the 21st century as an alternative to the very toxic Quantum Dots. Our lab is focused on the synthesis and study of their photo- and biophysical properties through well-established techniques such as UV Analysis, Fluorescence Analysis, Atomic Force Microscopy and the Langmuir Monolayer technique. Also we study the influence of Carbon Dots on protein aggregation-fibrillation.


Alpha-L-Fucosidase

In humans, a-L-fucosidase is a liver specific enzyme that is typically only present during gestation. Upon birth, production of this enzyme ceases and the serum levels found in healthy blood is mostly negligible. However, in individuals who develop hepatocellular carcinoma (the most common of all neoplasms of the liver), the enzyme begins to be synthesized again, allowing for early cancer diagnosis through detection of this biomarker. Our goal is to develop a simple, optical assay for the detection of this cancer biomarker, through the use of specific probed-antibodies immobilized onto a solid quartz surface.


Photodynamic Therapy

The lowest excited state of oxygen, singlet oxygen, has been shown to have promising results in medicinal purposes for many years. Typically, singlet oxygen is produced through irradiation of a photosensitizer, which are generally porphyrins, chlorophylls or dyes. Singlet oxygen possesses high reactivity towards a wide range of molecules, due to its strong oxidizing nature. This has led many to use it as a source of cancer treatment through selectively irradiating a tumorous area in the presence of a specific photosensitizer. Our goal is to use this approach externally, for treatments of MRSA and fungal infections found on the eye. Treatment outside the body allows for a wider range of possible photosensitizers to be used, as the irradiation source does not need to penetrate many layers of skin or flesh to reach the infected area.


Graphene Oxide

Graphene oxide (GO), a novel 2-dimensional carbon based nanomaterial, has shown potential applications in biomedical and biological field, including drug and gene delivery, sensing, and imaging However, one critical question needs to be addressed before any actual application: how does GO interact with biological molecules, such as proteins, enzymes and biomembranes? In our study, spectroscopy, microscopy, and surface chemistry are applied to fundamentally understand the nature of interactions between these molecules and GO.


Protein fibrillation

It has been known for several decades that failure to adopt or remain native conformations of some specific peptides or proteins can result in a wide range of human diseases. The pathological conditions of these diseases are now known to be commonly associated with protein misfolding processes. More than 20 human peptides or proteins have been found to be able to misfold and develop aberrant self-assemblies in vivo, which are characterized by conformational conversion of soluble peptides or proteins into insoluble amyloid-like fibrils. The misfolding peptides or proteins associated with serious human amyloidogenic diseases include amyloid-beta peptide in Alzheimer's disease (AD), islet amyloid polypeptide (IAPP) in type 2 diabetes, alpha-synuclein in Parkinson's disease (PD), and prion protein in the spongiform encephalopathies. We are interested in the kinetics and mechanisms of protein fibrillation of A-beta amyloid, IAPP, and human insulin.


Troponin I Biosensing

Troponin I ( cTnI ) is a protein of 209 amino acids found in the cardiac muscle tissue. Following a cardiac tissue damage ( i.e. following a heart attack ), this protein is released in the bloodstream from the broken cardiac cells. Quantitative Analysis of blood cTnI is a well-known method to confirm the occurrence of a heart attack. A reliable analytical procedure to determine cTnI on a picogram level is of great and urgent importance. Our goal is to develop the ultimate, reliable, reproducible and, most important, extremely specific and sensitive test for the determination of Troponin I through fluorescence techniques.