IMBB - WebCalendar

Time:

13:00

Location:

“Seminar Room 1”, FORTH’s bldg

Description:

IMBB SEMINAR

Dimitris BEIS
Investigator C (Assistant Professor level)
Zebrafish models of Human Disease
Biomedical Research Foundation, Academy of Athens

Title: "Zebrafish models of Human Disease".

Tuesday, April 19th 2016 @ 13:00
“Seminar Room 1”, FORTH’s bldg

Host: N. Tavernarakis

Time:

15:00

Location:

Computer Science Department, room A113 (ground floor), Voutes

Description:

MST colloquium
Tuesday, April 19, 2016

Speaker:Athina Bakopoulou
Affiliation:Dep. of Fixed Prosthesis & Implant Prosthodontics, School of Dentistry, Aristotle University of Thessaloniki

Title:Stem cells of oral origin: from bench to bedside

Location:Computer Science Department, room A113 (ground floor), Voutes
Time:15:00
Language: English

Abstract

Oral and dental diseases are major public health problems worldwide, with a profound effect onquality of life. Current treatment modalities are based on non-biological artificial substitutes, such as dental fillings, fixed and removable partial dentures supported by teeth and/or implants, complete dentures etc. These substitutes have several disadvantages, including uncomfortable sensation, insufficient biocompatibility, damage to the surrounding tissues and unpredictable long-term therapeutic efficacy.This provides exemplary justification for identifying regeneration of oral/dental tissues as the “ultimate goal” of current tissue engineering strategies in regenerative dentistry. The discovery and characterization of stem cells (SCs) from various oral sources, such as the dental pulp, periodontal ligament, dental follicle, apical papilla, oral mucosa, orofacial bones, salivary glands and other together with the cutting edge research of recent years in understanding their biology have enhanced our knowledge of the complex role of SCs in developmental/repair processes. The application of this knowledge in translational studies has been a decisive milestone in bringing these technologies closer to clinical application. Amazing technological advances, such as development of customized biomimetic scaffolds, fine tuning of the stem cell niche microenvironent by means of bioreactors and single-cell analysis possibilities by means of microfluidics have provided valuable tools in translating scientific advances into clinical settings. Finally, establishment of Good Manufacturing Practice-GMP protocols according to European regulations and establishment of clinical-grade, xeno-free stem cell lines have facilitated feasibility and “proof-of-concept” clinical trials on the application of oral SCs in orofacial or other tissue regeneration.
Most recently the potential to use the plethora of secreted throphic and immunomodulatory cytokines produced by SCs (known as secretome), as a therapeutic module instead of the cells has been proposed as a safer and effective alternative to SC transplantation highlighting the dilemma between stem cell vs. secretome therapy? This lecture will provide an overview of the biological properties of oral SCs, analyzing current research trends and critical milestones towards clinical application.

For forthcoming colloquia, please visit:
http://www.materials.uoc.gr/en/colloquia

Time:

14:00

Location:

FORTH Amphitheatre

Description:

InnovCrete Seminar

From Biological Self-Assembly to Novel Peptide Nanostructures of Unique Mechanical, Optical, Piezoelectric and Semiconductive Properties

Prof. Ehud Gazit, Tel Aviv University, ISRAEL

Wednesday, April 20, 2016 @ 14:00
FORTH Amphitheatre

Host: M. Kokkinidis

Time:

12:00

Location:

FORTH Amphitheatre

Description:

InnovCrete Seminar

Regulation of bacterial cell wall growth

Prof. Waldemar Vollmer, Newcastle University, UK

Thursday, April 21st, 2016 @ 12:00
FORTH Amphitheatre

Host: M. Kokkinidis

The bacterial cell envelope has a complex structure and must be enlarged when the cell grows and divides. Gram-negative bacteria have in their periplasm a mainly single-layered peptidoglycan sacculus that protects the cell from lysis due to the turgor and that is required to maintain cell shape. During growth and cell division the sacculus is enlarged by the coordinated activities of peptidoglycan synthases (penicillin-binding proteins, PBPs) and hydrolases, which presumably form dynamic multi-enzyme complexes. The molecular mechanisms of peptidoglycan growth and its regulation are poorly understood.
Cytoskeletal proteins and associated cell morphogenesis proteins control peptidoglycan synthesis from inside the cell, within large cell envelope assemblies called elongasome and divisome. Recent work showed that peptidoglycan growth is also regulated from outside the sacculus in Escherichia coli and likely other Gram-negative bacteria. The outer membrane lipoproteins LpoA and LpoB are required for the functioning of the main peptidoglycan synthases, PBP1A and PBP1B, respectively. Lpo proteins interact with their cognate PBP and activate the transpeptidase function in vitro. The Lpo-interaction occurs with small, non-catalytic domains that have co-evolved with the outer-membrane activators. Presumably, Lpo proteins regulate peptidoglycan synthesis form outside the sacculus to maintain a homogenous peptidoglycan surface density and thickness, and to fine-tune peptidoglycan growth rate. PBP1A-LpoA are mainly active during cell elongation, and PBP1B-LpoB are members of the divisome and provide the main peptidoglycan synthesis activity during cell division. I will present recent structural data showing how LpoA and LpoB are able to span the periplasm to interact with their cognate PBP. Recent data also show that PBP1B-LpoB are modulated by CpoB, a protein that is required to coordinate peptidoglycan synthesis with outer membrane constriction during cell division.

Time:

13:00

Location:

FORTH Amphitheatre

Description:

InnovCrete Seminar

NMR Insights on the conformational plasticity and interaction of biomolecules

Prof. George Spyroulias, Patras University, GREECE

Thursday, April 21st, 2016 @ 13:00
FORTH Amphitheatre

Host: M. Kokkinidis

The use of Modern Biomolecular NMR which is a powerful technique for the investigation of the conformational dynamics and structure-activity correlation of proteins and their complexes, provides atomic-level insights about the conformational dynamics of these biologicaly relevant molcules. To achieve this goal it is required the concerted action of molecular biology, spectroscopy and computational biology for the high-yield production of proteins in suitable forms for NMR studies (uniform labeling in 2H, 13C, 15N nuclei, and specific labeling of residues or chemical groups in 13C, 15N), the acquisition a series of NMR data and the determination of the 3D structures in solution along with the ellucidation of the relaxation properties of proteins with molecular weight ranging from 7 to >25 kDa.
Among our current research interests is the NMR-driven conformational dynamics study of disease-related enzymes and proteins, such as: (i) RNA binding proteins (~350 aminoacids) [1-2], which are key-factors in proper folding of pre-tRNA transcripts, like La autoantigen (ii) Heme-nitric oxide/oxygen binding (H-NOX) motifs (~200 amino acids), which exist as proteins or domains within larger proteins, such as soluble guanylate cyclase and function as a sensor for the gaseous signaling agent nitric oxide (NO) that regulates the catalytic site contained within the C-terminal end of the enzyme [3], (iii) macro domains (~170 aminoacids), which are evolutionarily conserved in eukaryotic organisms, bacteria and archaea and they are also found in nonstructural proteins (nsPs) of several positive-strand RNA viruses, including hepatitis E virus, rubella virus and coronaviruses, as well as alphaviruses [4-5], (iv) various E3 ubiquitin ligases involved in ubiquitination pathway, like ARKADIA tumor suppressor [6-7], (v) extracellular domains of ligand-gated ion channels of the cys-loop family (nAChR is the prototype) that involved in various neurodegenerative disorders [8], and others.

Time:

12:00

Location:

FORTH Amphitheatre

Description:

InnovCrete Seminar

How do proteins evolve?

Prof. Dan S. Tawfik, Weizmann Institute of Science, Israel

Friday, April 22nd, 2016 @ 12:00
FORTH Amphitheatre

Host: M. Kokkinidis

I will briefly describe our insights regarding how new enzymatic functions evolve, via gradual, small changes in sequence, and while preserving the overall structure (fold) and active-site architecture. However, the mechanisms underlying these evolutionary micro-transitions do not explain the macro evolutionary transitions – how completely new folds emerge, let alone how the very first protein(s) evolve. The latter are thought to have emerged from short polypeptides. I will describe our findings with respect to how functional, globular proteins may emerge from short peptides.

Time:

13:00

Location:

FORTH Amphitheatre

Description:

InnovCrete Seminar

Drug Design via XRPD: From a protein microcrystalline sample to experimental powder diffraction data and the derived structural model

Prof. Irene Margiolaki, Patras University, GREECE

Friday, April 22nd, 2016 @ 13:00
FORTH Amphitheatre

Host: M. Kokkinidis

The development of the X-ray powder diffraction (XRPD) methods and algorithms, has already allowed for the structural characterization of a range of proteins and has been established by our group as a useful complementary technique to the traditional single crystal diffraction techniques. Protein polycrystalline samples consist of a large number of randomly oriented microcrystals. They often form in a short period of time and under different conditions of physico - chemical environment. To date, our studies on Urate Oxidase and complexes of human insulin with organic ligands, revealed a high degree of polymorphism, as well as crystalline polymorphs which were not previously identified probably due to the lack of adequate tools to characterize microcrystalline protein precipitates. The aim of this talk is to describe the frontier of powder diffraction as it begins to make a significant impact on structural biology. Issues which will be discussed include: (a) application of the molecular replacement technique and structure refinements of selected proteins associated with pharmaceutical interest (b) high throughput investigations such as crystal screening and phase diagram mapping and (c) ligand binding.