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The Laboratory for Molecular Sensing
The main interest of the laboratory is on understanding the rules underlying the folding of proteins and how their structure is modified by the interaction with other proteins, nucleic acids and small ligand molecules. To approach these issues we use, and occasionally develop, new, advanced optical methodologies. The acquired knowledge in protein structure is used for the design of innovative diagnostic methods and for other biotechnology applications.
The focus is to develop and apply advanced luminescence methodologies and optical measurements to solve questions of biochemical and medical interests. In particular, our interests are focused on the study at a molecular level of the interactions involving proteins, enzymes, nuclei acids as well as small ligand molecules for contributing to shed light to the fields of proteomics, post-proteomics, interatomic and bio/sensing. Our lab is equipped with the state-of-art instrumentations for investigating biological interactions by means of FRET, time-resolved FRET, fluorescence polarization, anisotropy decays, fluorescence correlation spectroscopy for single molecule detection, surface plasmon resonance, circular dichroism in the far- and near-UV regions, stopped-flow methodologies, metal enhanced fluorescence. In addition, the Lab has core collaborations in the fields of bioinformatics, atomic force microscopy, linear spectroscopy, material engineering, and nanotechnology that allow us to handle research projects until they are completely fulfilled. The Lab is also active in the use of fluorescence to quantify structural features of biological molecules even at nano-scale, and, consequently, to design advanced optical biochips, Lab-on-Chip, or simple disposable biosensors for analyses of high social interest (POCT). This capability in biophysical methodologies together with expertise in protein biochemistry, molecular genetics and microbiology allows the research team to challenge cutting-edge biochemical questions as well as to rapidly answer to biotechnological requests from SMEs and public institutions.
Keywords: Protein structure and stability; Biosensors; Diagnostic tools; POCT;
Publications (Last five years)
171. Novel biosensors based on optimized glycine oxidase
168. An innovative biophotonic gas sensor for the ultra-sensitive detection of DMMP as a simulant of SARIN
161. Extending the range of FRET: the Monte Carlo study of the antenna effect.
159. Vesicular and non-vesicular glucosylceramide transport feed distinct glycosylation pathways
158. Fluorescence correlation spectroscopy and molecular dynamics simulations to study the structural futures of the maltotriose-binding protein from Thermus thermophilus
155. Amino acid transport in thermophiles: characterization of an arginine-binding protein from Thermotoga maritima. 4. A brief thermo-story
152. An Innovative Plastic Optical Fiber-based Biosensor for new Bio/applications. The Case of Celiac Disease
151. Detection of odorant molecules via surface acoustic wave biosensor array based on odorant-binding proteins
150. Under pressure that splits a family in two. The case of lipocalin family
148. A biophotonic sensor for the specific detection of DMMP vapors at the ppb level
147. Determination of benzyl methyl ketone, a commonly used precursor in amphetamine manufacture
143. Porous silicon wafer-based “lab on chip” sensor
142. A surface plasmon resonance-based biochip to reveal traces of ephedrine
141. D-Serine-Dehydratase from Saccaromyces cerevisiae. A Pyridoxal -5’-phosphate-Dependent Enzyme for Advanced Biotech Applications
136. New insight into protein-ligand interactions. The case of the D-galactose/D-glucose-binding protein from E. coli.
134. Absorption into fluorescence. A method to sense biologically relevant gas molecules
133. The archeal topoisomerase reverse girase is a helix-destabilizing protein that unwinds four-way DNA functions
128. Amino acid transport in thermophiles: characterization of an arginine-binding protein in Thermotoga maritima. 2. Molecular organization and structural stability
125. Human galectin-3 interacts with two anticancer drugs: a spectroscopic study
121. Pressure Effects on the structure and stability and of the hyperthermophilic trehalose/maltose-binding protein from Thermococcus litoralis
120. Tumor specific protein human galectin-1interacts with anticancer agents
119. FCS-based sensing for the detection of Ocratoxin A and Neomycin in food
117. Structure and stability of a rat odorant-binding protein. Another brick in the wall”
A strength of the Lab and associated personnel is their many years of experience in biochemistry/molecular genetics and fluorescence spectroscopy. This group collectively has 100 man/years of experience in fluorescence spectroscopy and biochemistry/ molecular genetics and has authored a large number of manuscripts on this topic. Actually, the Lab plays an important role in excellence networks of European labs for the physical-chemical characterization of biomolecules under severe conditions. The Lab is also member of several European Consortia for the development of frontier methodologies for monitoring food safety and homeland security and Point of Care Tests (PoCT).
To testify the high standard levels reached from the Lab, we are proud to announce that some of the research projects of the Lab have recently gained the front pages of nine international Journals.
On July 1st 2007 the American Chemical Society has published a RESEARCH PROFILE on the activity of the Lab (Analytical Chemistry 2007 July 1, page 4746) underlying the cutting-edge results obtained on the detection of traces gluten in food for celiac patients.
Patrizia Falabella – Associate Professor University of Basilicata
Paolo Ciambelli – Full Professor University of Salerno
Loredana Incarnato – Full Professor University of Salerno
Emiliano Descrovi – Associate Professor University of Turin
Dr. Marcella de Champdorè
Prof. Petr Herman