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Structural Biology Facility UPAT (SEE-DRUG)
Identification
Hosting Legal Entity
University of Patras
Address:
University Campus- Rio, PATRAS, PO: 26500 (Greece)
Location
University of Patras, Department of Pharmacy, Rio, Patras, PO: 26504 (Greece)
Structure
Type Of RI
Single-sited
Coordinating Country
Greece
Status
Status
Current Status:
Operational since 2013
Timeline
Being upgraded since 2017 to 2018
Operational since 2013
Under construction since 2011 to 2013
Design/planning since 2009 to 2011
Scientific Description
SEE-DRUG’s major aim is to strengthen and broaden the scientific reach and socio-economic impact of the University of Patras (UPAT) through the creation of a Regional Centre of Excellence for Structural Biology that emphasizes the characterization and development of bioactive molecules with therapeutic potential. SEE-DRUG takes advantage of UPAT’s pivotal strength and growth potential of Structural Biology and combines it with high-quality, multidisciplinary scientific expertise in Chemistry, Pharmacology, Biology and Bioinformatics. The SEE-DRUG project will enable: (a) the Protein Production group to efficiently produce and characterize protein drug-targets for structural analysis and drug development efforts, (b) the Structural Biology group to perform high-resolution structure determination, through time- and cost-effective NMR-based, cutting-edge techniques, and (c) the Pharmacology group to characterize lead therapeutic molecules in a comprehensive array of in vitro, ex vivo and in vivo systems.
Such a state-of-the-art centre will create a research ecosystem providing a number of positions for highly skilled scientists, engineers and for other qualified staff, and thus enhance scientific and economic growth both at a local and at a regional level, which will hopefully be sustained for years to come. It will also achieve the optimal integration of UPAT’s Structural Biology in ERA through the establishment of long-lasting partnerships, and will enhance the exchange of expertise and the building of networks with other scientists and technology end-users at a regional or local level, including the biopharmaceutical industry. Last, but not least, UPAT will provide knowledge, expertise and access to national, regional European and extra-European users or groups.

RI Keywords
X-ray crystallography, Confocal and Functional Microscopy, Biomolecular NMR, In-vitro/in-vivo/ex-vivo studies, 3D structures, Structural biology, Preclinical studies of pharmaceutical compounds, In-cell imaging
Classifications
RI Category
Structural Biology Facilities
Scientific Domain
Biological and Medical Sciences
ESFRI Domain
Health and Food
Services
Conformational studies & Structure Determination and interaction of proteins through NMR

Solution structure detrmination using NMR data and NMR-driven interaction studies monitored through 2D 1H-15N HSQC experiments. Secondary structure studies through Circular Dichroism

Qualitative/Quantitaive Analysis of biomarkers by NMR

NMR targeted and non-targeted metabolomics

Access to Equipment
High-Yield Protein production for Structural & Functional studies

High-Yield expression of recombinant proteins for structural and functional studies. 15N, 13C & 2H uniform, selective and segmental labeling of proteins for NMR stduies. Purification of proteins and physicochemical Characterization

Equipment
Confocal in cell imaging

The UPAT’s upgraded Confocal Microscopy Facility, is up to our knowledge unique in Greece for its capacities, properties and applications. This set up will allow the integration of the information gained on drug-target structures following their functional characterization. Insights from structural determination will be validated in live cells, to allow an understanding of how the biomolecule tested affects basic cellular pathways at the molecular levels. In addition, novel bioactive molecules will be evaluated for their efficacy in modulating protein target function and its signaling pathways.

Circular Dichroism Spectrometer

State of the art Circular Dichroism spectrometer, with capabilities for thermal unfolding/refolding of proteins

700 MHz high-field NMR spectrometer

700 MHz NMR spectrometer with a cryogenically cooled probe for enhanced sensitivity and four channels, in concert with uniformly or selectively enriched recombinant proteins (in 13C, 15N and 2H), allows the set up of various applications in the field of structural biology and drug design.

Robot crystal growth

A crystallization robot, unique in UPAT, is expected to provide new possibilities for crystallization trials and enhance efforts in Structure determination of proteins in crystals through X-ray diffraction.

Date of last update: 05/07/2018