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Contact details

Georgios A. Spyroulias, PhD.
Department of Pharmacy
University of Patras
Panepistimioupoli-Rion,
GR-26504 Patras, GREECE
Tel:    +30.2610.969950 (office)
+30.2610.969951 (terra silico)
+30.2610.969952 (terra vitro)
Fax:    +30.2610.969950
Email:  G.A.Spyroulias@upatras.gr

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Now is: 2017-11-21 21:25

nmr_studiesStructural Bioinformatics and Cheminformatics are related to the design, molecular modeling & docking, molecular dynamics simulation, database searching, prediction and analysis  of biomolecular structures and have many applications not only in biotechnology and medicinal chemistry but also in basic science. They both use the current knowledge and all available data in structural biology to link them with function and to test many hypotheses in biology. Specifically, Structural Biinformatics and Cheminformatics attempt to: (a) predict, by computer simulations, an amino acid sequence that would produce a protein with targeted properties, (b) build by comparative modeling new 3D protein models and complex structures, (c) study the conformational dynamics of small proteins or peptides and their complexes that are hard to be captured by any wet biology experiment (d) predict binding poses and screen small-molecules (ligands, substrates or drug candidates) towards protein targets.

The group performs structure and sequence analysis, data mining and applies molecular modeling techniques to explore peptide/protein sequence, structure and function. Computational methods such as homology modeling, molecular dynamics and docking simulation are used in order to monitor protein-protein/substrate interactions as a function of time. Through these computational methodologies the group aims to understand the biologically-relevant features in peptide/protein sequence and function in order to: (i) gain insights into the determinants of ligand binding events and selectivity, (ii) illuminate the nature of many disease-related mutations by mapping effects of molecular defects on 3D protein complex structures, including inter-complex protein-protein interaction, (iii) engineere and design of new protein sequence, bioactive peptides and/or inhibitors and (iv) assists the sequence comparison between proteins with unknown and known structure, which share sequence, topology and/or function similarities with the aim to exploit these data to the production of polypeptide domains through cloning and expression in E. coli or through solid phase chemical synthesis.

The group also established an approach for virtual screening process towards the quest of lead-molecules with biological activity towards protein/enzyme targets. This methodology incorporates the in silico design, evolution and evaluation of combinatorial libraries of compounds (from 10 to >104) using as building groups protein or non-protein amino acids, organic moieties, chelating groups, etc). Computational tools in the high-throughput screening of chemical libraries towards a target molecule using docking simulations are usually correlated with biological  data and result to the evaluation and optimization of structural and/or biological properties of the lead-molecules.