Our activities lie at the interface of chemistry, biology and engineering. Enzyme & Synthetic Biotechnology (ESB) is a multi-disciplinary group employing researchers with different types of expertise, such as molecular biology, engineering, chemistry and agricultural sciences. The main goal of ESB is the development of engineered microbial cells with the ability to perform novel and complex functions by employing principles of Synthetic Biology. The lab utilizes simple organisms, such as the bacterium Escherichia coli, the yeasts Saccharomyces cerevisiae and Pichia pastoris, and the microalgae Spirulina platensis and Nannochloropsis as “biological chassis” and seeks to evolve them into efficient “cell factories” for the production of valuable chemical and biological products, and for the performance of industrially important processes, such as drug sensing and discovery, biotransformations etc. Genetic engineering techniques are applied in order to redesign and rearrange the genome of the organism of interest, while protein engineering (directed protein evolution) and synthetic biology approaches are utilized so as to introduce novel functions in the cell. A key aspect of the work that is carried out is the design and development of high-throughput screening systems, which are used to isolate the rare biomolecules and microbial strains that execute the desired function among large combinatorial libraries comprising hundreds of millions of variants.
Dr. Georgios Skretas, was awarded a Consolidator Grant from the European Research Council (ERC) to develop engineered bacteria that accelerate drug discovery against diseases caused by protein misfolding. [Read more]
Permanent staff Dr. Georgios Skretas, Research Associate Professor / PhD in Chemical Engineering, Princeton University, USA Dr. Theodoros G. Sotiroudis, Researcher Emeritus / PhD in Chemistry, National & Kapodistrian University of Athens, Greece
Dr. Dimitra Zarafeta, PhD in Chemical Engineering, National Technical University of Athens, Greece
Dr. Dafni Delivoria, PhD in Chemical Engineering, National Technical University of Athens, Greece
Dr. Anastasia Galanopoulou, PhD in Biology, National & Kapodistrian University of Athens, Greece
Dr. Maria Tsekrekou, PhD in Biology, University of Crete, Greece
Mrs. Myrsini Michou,
MSc in Systems Biology, Agricultural University of Athens, Greece
PhD fellowship from the State Scholarships Foundations (IKY)
Mrs. Maria Giannakou,
MSc in National & Kapodistrian University of Athens, Greece
PhD fellowship from the State Scholarships Foundations (IKY)
Mrs. Elena Vasilopoulou,
MSc in Systems Biology, Agricultural University of Athens, Greece
PhD fellowship from the State Scholarships Foundations (IKY)
Mr. Aristeidis Michoglou-Sergiou,
MSc in Biochemistry, University of Crete, Greece
Mrs. Awa Diop,
MSc in Biochemistry, Agricultural University of Athens, France
Mrs. Spyridoula Krikoni,
MSc in Molecular Medicine, National & Kapodistrian University of Athens, Greece
Mrs. Nikoletta Karampetsou,
M.Sc. in Molecular Genetics, University of Leicester, UK
Mrs Eftichia Karyda, BSc in Biological Applications and Technologies, University of Ioannina, Greece
Prof. Hülya Karaca Gencer, Anadolou University, Turkey
Engineered bacteria as an early-stage drug discovery platform for diseases caused by protein misfolding & aggregation
It has been widely recognized that many incurable diseases with an enormous socioeconomic impact, such as Alzheimer’s disease, Parkinson’s disease, amyotrophic lateral sclerosis, type 2 diabetes etc., are initiated by a common molecular mechanism: the misfolding of specific proteins. With the ultimate goal of identifying compounds with potentially therapeutic effects against these disorders, we have developed a highly versatile synthetic biology platform for discovering macrocyclic rescuers of disease-associated protein misfolding. In this system, large combinatorial libraries of cyclic oligopeptides (>200 million members) are biosynthesized in Escherichia coli cells and simultaneously screened for their ability to rescue disease-associated protein misfolding using an ultrahigh-throughput genetic screen. Hit compounds identified by this screen, are subjected to more detailed evaluation by biochemical and biophysical methods of protein analysis, and their ability to inhibit protein misfolding-induced pathogenicity is evaluated using appropriate mammalian cell assays and in vivo models of the disease of interest. Medicinal chemistry approaches are subsequently employed to optimize the biological properties of the bioactive macrocycles in order to generate therapeutic leads against the target diseases.
Schematic representation of our engineered bacterial platform for the discovery of macrocyclic rescuers of MisP misfolding and aggregation. MisP: misfolding-prone protein; pMisP-GFP: plasmid encoding a MisP-GFP fusion;pSICLOPPS-NuX1X2X3-X6: vector library encoding the combinatorial library of cyclic oligopeptides P: sorting gate.
We are currently targeting the following proteins involved in misfolding diseases:
(top, left) Chemical structures of the selected cyclic pentapeptides ΑβC5-34 and ΑβC5-116; (top, right) TEM images of aged Αβ42 solutions in the presence and absence of the selected cyclic pentapeptides ΑβC5-34 and ΑβC5-116; (bottom, left) Paralysis of C. elegans worms expressing human Αβ in their body wall muscles under the control of a heat-inducible promoter, in the absence and presence of the selected cyclic oligopeptides ΑβC5-34 and ΑβC5-116; (bottom, right) Fluorescence microscopy images of C. elegans nematodes showing reduced formation of Αβ aggregates when treated with two of our selected cyclic pentapeptides ΑβC5-34 and ΑβC5-116. Taken from Matis, I. et al., Nature Biomedical Engineering, 2017.
(top, left) Structure of homodimeric SOD1 (taken from Banci, L. et al., Proc Natl Acad Sci USA, 2009); (bottom, left) Chemical structure of the selected cyclic pentapeptide SOD1C5-4; (top, right) Circular dichroism spectra of SOD1(A4V) incubated with/without the selected cyclic pentapeptides SOD1C5-4, ΑβC5-34 or ΑβC5-116 at room temperature for 90 d (1:1 and 5:1 indicate cyclic peptide:SOD1(A4V) molar ratios). Taken from Matis, I. et al., Nature Biomedical Engineering, 2017; (bottom, right) ΗΕΚ293 cells transiently expressing SOD1-GFP or SOD1(A4V)-GFP in the absence and presence of the selected peptide SOD1C5-4 or the Αβ-targeting cyclic pentapeptide ΑβC5-34, and visualized by confocal microscopy.
p53 & Cancer
Conformational stabilization of the DNA-binding (core) domain of the carcinogenic, misfolding-prone p53 variant Y220C by a selected cyclic oligopeptide as revealed by molecular dynamics simulations (collaboration with Dr. Manthos G. Papadopoulos)
We have identified hundreds of head-to-tail cyclic oligopeptide sequences that inhibit the misfolding and aggregation of Αβ. For four of them, termed ΑβC5-34, ΑβC5-116, ΑβC7-1 and ΑβC7-14 we have shown that they interfere with the normal course of Aβ aggregation and the formation of typical Aβ fibrils, generating species with reduced binding to the neuronal surface and reduced cytotoxicity in vitro and in vivo.
We have identified hundreds of head-to-tail cyclic oligopeptide sequences that inhibit the misfolding and aggregation of mutant human SOD1, associated with familial forms of ALS. For one of them, termed SOD1C5-4, we have shown that it interferes with the normal course of mutant SOD1 aggregation and the formation of typical mutant SOD1 aggregates in vitro. We have found that SOD1C5-4 is cell-permeable and that it reduces the formation and cytotoxicity of mutant SOD1 aggregates in human cell lines.
Delivoria, D. C., Chia S., Habchi, J., Perni, M., Matis, I., Papaevgeniou, N., Chondrogianni, N., Dobson, C. M., Vendruscolo, M., Skretas, G.* 2019. Bacterial production and direct functional screening of expanded molecular libraries for discovering inhibitors of protein aggregation. Science Advances. 5: eaax5108 [Read more]
Matis, I., Delivoria, D.C., Mavroidi, B., Papaevgeniou, N., Panoutsou, S., Bellou, S., Papavasileiou, K.D., Linardaki, Z., Stavropoulou, A.V., Vekrellis, K., Boukos, N., Kolisis, F.N., Gonos, E.S., Margarity, M., Papadopoulos, M.G., Efthimiopoulos, S., Pelecanou, M., Chondrogianni, N., Skretas, G*. 2017. An integrated bacterial system for the discovery of chemical rescuers of disease-associated protein misfolding. Nature Biomedical Engineering. 1, 838–852. [doi:10.1038/s41551-017-0144-3] [Read more]
News & Views commentary in Nature Biomedical Engineering: [Read more]
Skretas, G. Macrocyclic rescuers for disease-associated protein misfolding. PCT/IB2018/000622
Skretas, G. and Delivoria, D.C. Cyclic peptide inhibitors of amyloid-β aggregation. HIPO/20190100453
Prof. Michele Vendruscolo, Centre for Protein Misfolding Diseases, Department of Chemistry, University of Cambridge, UK
Dr. Niki Chondrogianni, Institute of Chemical Biology, National Hellenic Research Foundation, Greece
Dr. Maria Pelecanou, Institute of Biosciences and Applications, National Scientific Research Center “Demokritos”, Greece
Dr. Kostas Vekrellis, Biomedical Research foundation of the Academy of Athens, Greece
Prof. Spiros Efthimiopoulos, Department of Biology, National and Kapodistrian University of Athens, Greece
Dr. Manthos G. Papadopoulos, Institute of Chemical Biology, National Hellenic Research Foundation, Greece
Development of specialized microbial strains for high-level production of recombinant membrane proteins
Membrane proteins (MPs) perform critical cellular functions in all living organisms and constitute major targets for drug discovery. Escherichia coli has been the most popular overexpression host for membrane protein biochemical/structural studies. Bacterial production of recombinant membrane proteins, however, is typically hampered by poor cellular accumulation and severe toxicity for the host, which leads to low final biomass and minute volumetric yields. We have recently demonstrated that it is possible to rewire the E. coli protein-producing machinery so that it can withstand the toxicity caused by membrane protein overexpression, and that engineered bacterial strains with the ability to achieve high-level MP production can be generated. To achieve this, we searched for bacterial genes whose co-expression can suppress membrane protein-induced toxicity and identified two highly potent effectors: the membrane-bound DnaK co-chaperone DjlA, and the inhibitor of the mRNA-degrading activity of the E. coli RNase E RraA. We have generated two new E. coli strains co-expressing either djlA or rraA, which we have named SuptoxD and SuptoxR, respectively, and we have shown that these new strains accumulate markedly higher levels of final biomass and produce dramatically enhanced yields for a variety of prokaryotic and eukaryotic recombinant membrane proteins. In most cases that we have tested so far, either SuptoxD, or SuptoxR, or both, outperform the capabilities of commercial strains frequently utilized for recombinant membrane protein production purposes, such as C41(DE3), C43(DE3) and Lemo21(DE3).
Recombinant membrane protein production in the engineered E. coli strains SuptoxD and SuptoxR. (top, left) Schematic representation of a constructed fusion of the human bradykinin receptor 2 (BR2) with GFP; (top, center) Fluorescence of E. coli MC1061 (wild-type, WT) and SuptoxD cells expressing the BR2-GFP fusion; (top, right) Purification of fusion-free and detergent-solubilized BR2 from E. coli MC1061 (WT) and SuptoxD cells; (bottom, left) Comparison of the accumulation levels of a variety of eukaryotic and prokaryotic recombinant recombinant membrane proteins in E. coli MC1061 (WT) with SuptoxD and SuptoxR cells; (bottom, right) Comparison of the fluorescence of SuptoxD and SuptoxR cells producing chimeric fusions of the human bradykinin receptor 2 (BR2) and the human central cannabinoid receptor (CB2) with GFP with the fluorescence of equal culture volumes of C41(DE3), C43(DE3), and Lemo21(DE3) cells producing the same proteins.
We have developed the first set of engineered bacterial strains, termed E. coli SuptoxD and SuptoxR, with a general ability to suppress the cytotoxicity caused by the overexpression of recombinant membrane proteins.
Either SuptoxD, or SuptoxR, or both, have been found to outperform the capabilities of commercial strains frequently utilized for recombinant membrane protein production purposes, such as C41(DE3), C43(DE3) and Lemo21(DE3) in the cases that we have tested.
SuptoxD and SuptoxR are commercially available form EnzyQuest.
We are currently developing second-generation E. coli SuptoxD/R strains (SuptoxD2.0 & SuptoxR2.0) achieving further enhanced levels of recombinant membrane protein production.
Michou, M., Kapsalis, C., Pliotas, C., Skretas, G.* 2019. Optimization of recombinant membrane protein overexpression in the engineered Escherichia coli strains SuptoxD and SuptoxR. ACS Synthetic Biology. 8(7):1631-1641. [Read more]
Gialama, D., Kostelidou, K., Michou, M., Delivoria, D.C., Kolisis, F.N., Skretas, G*. 2017. Development of Escherichia coli strains that withstand membrane protein-induced toxicity and achieve high-level recombinant membrane protein production. ACS Synthetic Biology. 6(2): 284-300. [Read more]
Gialama, D., Delivoria, D.C., Michou, M., Giannakopoulou, A., Skretas, G*. 2017. Functional requirements for DjlA- and RraA-mediated enhancement of recombinant membrane protein production in the engineered E. coli strains SuptoxD and SuptoxR. Journal of Molecular Biology. 429(12):1800-1816. [Read more]
Michou, M., Stergios, A., Skretas, G.*. SuptoxD2.0: A second-generation Escherichia coli SuptoxD strain achieving further enhanced recombinant membrane protein production. In preparation
Vasilopoulou, E., Giannakopoulou, A., Skretas, G.*. SuptoxR2.0: A second-generation Escherichia coli SuptoxR strain with improved efficiency in enhancing recombinant membrane protein production.
Skretas, G. and Gialama, D. Systems for recombinant protein production. PCT/EP2017/025168
Dr. Christos Pliotas, Astbury Centre for Structural Molecular Biology, University of Leeds, UK
Prof. Terry K. Smith, School of Biology, University of St. Andrews, UK
Discovery of thermostable hydrolytic enzymes of industrial interest using functional (meta)genomics & bioinformatics
Enzymes are biocatalysts used in a wide range of “white biotechnology” applications. Hydrolases, a specific class of enzymes, have received great attention due to their high selectivity, potential synthetic ability and broad range of applicability, especially in the production of fine chemicals and pharmaceuticals. Despite their advantages, a very limited number of hydrolases are currently being used in the industry. This is due to the fact that many industrially relevant processes require high temperatures where conventional biocatalysts perform poorly. For such processes, thermo- or hyperthermostable enzymes are required. Thermophilic organisms are a potential rich source of such enzymes, which, however, remains largely unexplored. To address this, we apply systematic genomic and metagenomic screening approaches to identify novel hydrolases from microorganisms residing in extreme environments around the globe.
We have discovered and characterized biochemically and structurally a new thermostable and highly halotolerant GH5 cellulase (CelDZ1)
We have discovered a thermostable esterolytic enzyme (EstDZ2) that defines a new family of bacterial esterases (Family XV)
We have discovered and characterized biochemically and structurally one of the most thermostable esterolytic enzymes described to date (EstDZ3)
We have discovered and characterized biochemically a new thermostable xylanase (XynDZ5)
Zarafeta, D., Galanopoulou, A., Kaili, S., Chegkazi, M.S., Chrysina, E.D., Kolisis, F.N., Hatzinikolaou, D.G.*, Skretas, G.* 2019. XynDZ5: A new thermostable GH10 xylanase. Frontiers in Microbiology. In revision.
Giannakopoulou, A., Patila, M., Spyrou, K., Chalmpes, N., Zarafeta, D., Skretas, G., Gournis, D., Stamatis, H.* 2019. Development of a Four-Enzyme Magnetic Nanobiocatalyst for Multi-Step Cascade Reactions. Catalysts. 9: 995. [Read more]
Wohlgemuth, R.*, Littlechild, J., Monti, D., Schnorr, K., Siebers, B., Menzel, P., van Rossum, T., Kublanov, I., Rike, A.G., Skretas, G., Szabo, Z., Peng, X., Young, M. 2018. Discovery of Novel Hydrolases from Hot Environments. Biotechnology Advances. 36(8): 2077-2100. [Read more]
Ladoukakis, Ε., Koutsandreas, Τ., Pilalis, Ε., Zarafeta, D., Kolisis, F.N., Skretas, G., Chatziioannou, A.* 2019. ANASTASIA: a distributed pipeline for automated integration, analysis and functional characterization of next-generation sequencing metagenomic datasets. Frontiers in Genetics. 10:469. [Read more]
Zarafeta, D., Moschidi, D., Ladoukakis, E., Gavrilov, S., Chrysina, E.D., Chatziioannou, A., Kublanov, I., Skretas, G.*, Kolisis, F. N.*. 2016. Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases. Scientific Reports. 6: 38886. [Read more]
Zarafeta, D., Szabo, Z., Moschidi, D., Phan, H., Chrysina, E.D., Peng, X., Ingham, C.J., Kolisis, F. N.*, Skretas, G.*. 2016. EstDZ3: a new esterolytic enzyme exhibiting remarkable thermostability. Frontiers in Microbiology. 7: 1779. [Read more]
Zarafeta, D., Kissas, D., Sayer, C., Gudbergsdottir, S. R., Ladoukakis, E., Isupov, M. N., Chatziioannou, A., Peng, X., Littlechild, J. A.*, Skretas, G.*, and Kolisis, F. N.* 2016. Discovery and characterization of a thermostable and highly halotolerant GH5 cellulase from an Icelandic hot spring isolate. PLoS One, 11(1): e0146454. [Read more]
Prof. Fragiskos Kolisis, School of Chemical Engineering, National Technical University of Athens, Greece
Dr. Aristotelis Chatziioannou, Institute of Chemical Biology, National Hellenic Research Foundation, Greece
Prof. Xu Peng, Department of Biology, University of Copenhagen, Denmark
Dr. Ilya Kublanov, Department of Microbial Communities, Winogradsky Institute of Microbiology, Russia
Prof. Jennifer A. Littlechild, College of Life and Environmental Sciences, University of Exeter, UK
Prof. Dimitris Hatzinikolaou, Department of Biology, National & Kapodistrian University of Athens, Greece
Dr. Evangelia Chrysina, Institute of Chemical Biology, National Hellenic Research Foundation, Greece
Prof. Haris Stamatis, Department of Biological Applications and Technologies, University of Ioannina, Greece
Prof. Ioulia Smonou, Department of Chemistry, University of Crete, Greece
Development of protein-based tools for synthetic biology applications in biosensing and the programming of cell behavior
E. coli cells producing one of our engineered protein-based thyroid hormone sensors and grown in the absence or presence of triiodothyronine (T3) at different incubation temperatures. Taken from Skretas and Wood, Protein Science, 2005.
We have generated the first bacterial biosensors with the ability to detect the presence of human hormones
Our engineered biosensors can discriminate between the action of hormone agonists and antagonists
We have used one of our engineered biosensors to perform chemical library screening for the discovery of new selective estrogen receptor modulators
Skretas, G.*, Meligova, A., Villalonga-Barber, C., Mitsiou, D.J., Alexis, M.N., Micha-Screttas, M., Steele, B.R., Screttas, C.G., and Wood, D.W*. 2007. Engineered chimeric enzymes as facile tools for pharmaceutical discovery: Construction of simple bacterial screens for the detection, discovery and assessment of estrogen receptor modulators. Journal of the American Chemical Society. 129: 8443-8457. [Read more]
Skretas, G., and Wood, D.W.* 2005. Rapid detection of subtype-selective nuclear hormone receptor binding with bacterial genetic selection. Applied and Environmental Microbiology. 71: 8995-8997. [Read more]
Skretas, G., and Wood, D.W.* 2005. A bacterial biosensor of endocrine modulators. Journal of Molecular Biology. 349: 464-474. [Read more]
Skretas, G., and Wood, D.W.* 2005. Regulation of protein activity with small-molecule-controlled inteins. Protein Science. 14: 523-532. [Read more]
Wood, D.W. and Skretas, G. Bacterial ligand-binding sensor. United States Patent 7592144
Prof. David W. Wood, Department of Chemical and Biomolecular Engineering, The Ohio State University, USA
Dr. Michael N. Alexis, Institute of Chemical Biology, National Hellenic Research Foundation, Greece
Peptides and proteins of microalgae and Greek olive products
We have shown that virgin olive oil endogenous amphiphiles (including proteins) stabilize olive oil-in water emulsions.
We have shown that phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin.
We have discovered and characterized biochemically a melanin and humic acid-like polymer complex from olive mill waste waters.
We have discovered and characterized biochemically heat-stable lipolytic enzyme activities of the marine alga Nannochloropsis oceanica.
Sotiroudis, T.G., Sotiroudis, G.T., Varkas, N., Xenakis, A. 2005. The role of endogenous amphiphiles on the stability of virgin olive oil-in-water emulsions. J. Amer. Oil Chem. Soc. 82, 415-420 (2006 Archer Daniels Midland /Protein and Co-Products Division Best Paper award in the Chemistry and Nutrition category of the American Oil Chemists’ Society).
Tzika, E.D., Sotiroudis, T.G., Papadimitriou, V., Xenakis, A. 2009. Partial purification and characterization of peroxidase from olives (Olea europaea cv.Koroneiki). Eur. Food Res. Technol. 228, 487-495.
Xenakis, A., Papadimitriou, V., Sotiroudis, T.G. 2010. Colloidal structures in natural oils. Curr. Opin. Colloid Interface Sci. 15, 55-60.
Tzika, E., Christoforou, M., Pispas, S., Zervou,M., Papadimitriou, V., Sotiroudis, T.G., Leontidis, E. Xenakis, A. 2011. Influence of nanoreactor environment and substrate location on the activity of horseradish peroxidase in olive oil-based w/o microemulsions. Langmuir, 27, 2692-2700.
Papadimitriou, V., Tzika, E. D., Pispas, S., Sotiroudis, T. G. Xenakis, A. 2011. Microemulsions based on virgin olive oil: a model biomimetic system for studying native oxidative enzymatic activities. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 382, 232-237.
Parages, M.L., Rico, R.M., Abdala-Díaz, R.T., Chabrillón, M., Sotiroudis, T.G., Jiménez, C. 2012. Acidic polysaccharides of Arthrospira (Spirulina) platensis induce the synthesis of TNF-α in RAW macrophages, J. Appl. Phycol. 24, 1537-1546.
Sotiroudis, T.G., Sotiroudis G.T. 2013. Health aspects of Spirulina (Arthrospira) microalga food supplement. J. Serb. Chem. Soc. 78, 395-405.
Kyriazi, A., Papadimitriou, V., Sotiroudis, T.G., Xenakis, A. 2013. Development and characterization of a digestion model based on olive oil microemulsions. Eur. J. Lip. Sci. Technol. 115, 601-611.
Minic, S.L., Milcic, M., Stanic-Vucinic, D., Radibratovic, M., Sotiroudis, T.G., Nikolic, M.R., Cirkovic Velickovic, T. 2015. Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin. RSC Adv.5, 61787-61798
Markou, G., Iconomou, D., Sotiroudis T., Israilides, C., Muylaert, K. 2015. Exploration of using stripped ammonia and ash from poultry litter for the cultivation of the cyanobacterium Arthrospira platensis and the green microalga Chlorella vulgaris. Bioresour. Technol. 196, 459-468.
Khemakhem, M., Papadimitriou, V., Sotiroudis, G., Zoumpoulakis, P., Arbez- Gindre, C., Bouzouita, N., Sotiroudis, T.G. 2016. Melanin and humic acid-like polymer complex from olive mill waste waters. Part I. Isolation and characterization. Food Chem. 203, 540-547.
Khemakhem, M., Sotiroudis, G., Mitsou, E., Avramiotis, S., Sotiroudis, T.G., Bouzouita, N., Papadimitriou, V. 2016, Melanin and humic acid-like polymer complex from olive mill waste waters. Part II. Surfactant properties and encapsulation in W/O microemulsions. J. Mol. Liq. 222, 480-486.
Savvidou, M.G., Lymperopoulou, T.V., Mamma, D., Balta-Brouma, K.P., Sotiroudis,T.G., Kekos, D., Kolisis, F.N. 2017. A study on the combined eﬀects of carbon and nitrogen source on high added value products synthesis by Nannochloropsis oceanica CCMP1779 using response surface methodology. Biocatal. Agric. Biotechnol. 10, 298-307
Prof. Fragiskos Kolisis, School of Chemical Engineering, National Technical University of Athens, Athens, Greece
Dr. Aristotelis Xenakis, Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece
Dr. Vassiliki Papadimitriou, Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece
Prof. Ioanna Chinou, Department of Pharmacognosy and Natural Product Chemistry, Faculty of Pharmacy, National and Kapodistrian University of Athens, Athens, Greece
Prof. Tanja Ćirković-Velickovic, Department of Biochemistry, Center of Excellence for Molecular Food Sciences, Faculty of Chemistry, University of Belgrade, Belgrade, Serbia
Prof. Nabiha Bouzouita, École Superieure des Industries Alimentaires de Tunis, Tunis, Tunisia
Dr. Cleanthes Israelides, Department of Biotechnology of Agricultural Products, Institute of Technology of Agricultural Products, Hellenic Agricultural Organization-Demeter, Athens, Greece
Dr. Carlos Jiménez, Departamento de Ecología, Facultad de Ciencias, Universidad de Málaga, Málaga, Spain
Dr. Panagiotis Zoumpoulakis, Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece
Dr. Milan R. Nikolic, Department of Biochemistry, Center of Excellence for Molecular Food Sciences, Faculty of Chemistry, University of Belgrade, Belgrade, Serbia
Dr. Maria Zoumpanioti, Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece
Dr. Cecile Arbez-Gindre, Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece
George Sotiroudis, Msc., Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece
Participation in International Scientific Networks
COST Action BM1405 | Non-globular proteins - from sequence to structure, function and application in molecular physiopathology (NGP-NET) | 26 March 2015 - 25 March 2019. Dr. Georgios Skretas is serving as a Management Committee.
COST Action BM1307 | European network to integrate research on intracellular proteolysis pathways in health and disease (PROTEOSTASIS) | 25 April 2014 - 24 April 2018. Dr. Georgios Skretas is serving as the 1st substitute Management Committee member for Greece.
COST Action CM1303 | Systems Biocatalysis (SysBioCat) | 20 November 2013 - 19 November 2017. Dr. Georgios Skretas served as the 1st substitute Management Committee member for Greece.
European research network ERA-Net “Synthetic Biology” (ERA-Synbio). Dr. Georgios Skretas has served as a Representative of the General Secretariat of Research and Technology of Greece to meetings and workshops.