Biomedical subjects

Vicky Vamvakaki

Publications and source records attributed to Vicky Vamvakaki.

5 recordsLinked to original sources

PubMed2007

Pesticide detection with a liposome-based nano-biosensor.

Monitoring of the organophosphorus pesticides dichlorvos and paraoxon at very low levels has been achieved with liposome-based nano-biosensors. The enzyme acetylcholinesterase was effectively stabilized within the internal nano-environment of the liposomes. Within the liposomes, the pH sensitive fluorescent indicator pyranine was also immobilized for the optical transduction of the enzymatic activity. Increasing amounts of pesticides lead to the decrease of the enzymatic activity for the hydrolysis of the acetylcholine and thus to a decrease in the fluorescent signal of the pH indicator. The decrease of the liposome biosensors signal is relative to the concentration of dichlorvos and paraoxon down to 10(-10)M levels. This biosensor system has been applied successfully to the detection of total toxicity in drinking water samples. Also a colorimetric screening device for pesticide analysis has been evaluated.

Biosensing Techniques↗

PubMed2006

Immobilization of enzymes into nanocavities for the improvement of biosensor stability.

Nanoporous materials with different pore sizes are evaluated as immobilization and stabilization matrices of proteins for the development of highly stable biosensors. It has been proven experimentally that confinement of proteins in cages with a diameter that is 2-6 times larger than their size increases considerably the stability of the biomolecules, as has been shown earlier by theoretical calculations. Porous silica beads with pore sizes of 10nm were utilized for the immobilization of the enzymes HRP and GOx with diameters in the order of 5 and 7 nm, respectively. The sensitivity of the corresponding biosensor systems was monitored for 70 h under continuous operation conditions (+600 mV) and it was found that the stabilization factor of GOx is 1.7 times higher compared to HRP. Also the stabilization efficiency of enzymes against leaching and inactivation in porous polymer beads with pore diameters of 10 and 30 nm was examined. The leaching rate of the enzyme AChE from the 30 nm polymer beads was found to be 1.1 times higher than that from the 10nm beads. At the same time the remaining activity of GOx biosensors after 5 days of continuous operation conditions (+600 mV) was found to be 2.1 times higher when the enzyme had been immobilized in the 10nm beads compared to the 30 nm beads. It is thus evident that the matching between the pore size of nanoporous materials and the molecular size of enzymes is essential for the development of biosensors with extended shelf and operational lifetimes.

Biosensing Techniques↗

PubMed2006

Carbon nanofiber-based glucose biosensor.

The use of highly activated carbon nanofibers for the design of catalytic electrochemical biosensors is demonstrated. The direct immobilization of enzymes onto the surface of carbon nanofibers is shown to be a highly efficient method for the development of a new class of very sensitive, stable, and reproducible electrochemical biosensors. These results establish the fact that the carbon nanofiber is the best matrix so far described for the development of biosensors, far superior to carbon nanotubes or graphite powder.

Biosensing Techniques↗

PubMed2005

Stabilization of enzymes in nanoporous materials for biosensor applications.

In this study we present the results obtained from efforts to stabilize the inherently unstable m-AChE in nanoporous materials, for the development of biosensors with increased operational stability. Based on existing theoretical models, the entrapment of proteins into relatively small rigid cages drastically increases the stability of these proteins, as this is manifested by their decreased tendency to unfold. The use of two different meso/nanomaterials for the immobilization of the m-AChE shows that there is both a decrease in the leaching of the protein from the biosensor membrane to the test solution, as well as a drastic increase in the operational stability of the resulting biosensor.

Acetylcholinesterase↗

PubMed2004

Fluorescence detection of enzymatic activity within a liposome based nano-biosensor.

The encapsulation of enzymes in microenvironments and especially in liposomes, has proven to greatly improve enzyme stabilization against unfolding, denaturation and dilution effects. Combining this stabilization effect, with the fact that liposomes are optically translucent, we have designed nano-sized spherical biosensors. In this work liposome-based biosensors are prepared by encapsulating the enzyme acetylcholinesterase (AChE) in L-a phosphatidylcholine liposomes resulting in spherical optical biosensors with an average diameter of 300+/-4 nm. Porins are embedded into the lipid membrane, allowing for the free substrate transport, but not that of the enzyme due to size limitations. The enzyme activity within the liposome is monitored using pyranine, a fluorescent pH indicator. The response of the liposome biosensor to the substrate acetylthiocholine chloride is relatively fast and reproducible, while the system is stable as has been shown by immobilization within sol-gel.

Acetylcholinesterase↗