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| Azobenzénové deriváty ako potenciálne terapeutiká pre Alzheimerovu chorobu | |
| Azobenzenes as potential Alzheimer\’s theranostic agents | |
| Program: | Mobility |
| Project leader: | RNDr. Bednáriková Zuzana, PhD. |
| Annotation: | Amyloid fibrils of amyloid β (Aβ) peptides are a neuropathological feature of Alzheimer\’s disease (AD). AD is one of the world\’s fastest-growing neurological diseases with substantial economic and societal impact, but no cure is currently available. Therefore, the exploration of novel treatment approaches is in high demand. The project\’s main objective is to study the ability of azobenzene molecules to affect targets associated with the amyloid cascade of AD pathogenesis. The project will employ the lever-like potential of azobenzene molecules to dissociate fibrillar aggregates of Aβ peptides and inhibit the proteolytic activity of β-secretase. We will integrate in vitro, in silico, and cells workflow to find a possible alternative therapy against this devastating disease. Moreover, this collaborative research partnership will present an excellent opportunity for both teams\’ young members to learn new techniques in the well-equipped laboratories at the Polish and Slovak Academies of Sciences and gain new experience by working in an international scientific environment. |
| Duration: | 1.1.2023 – 31.12.2024 |
| ANOMATY – Interakcie amyloidných fibríl a nanočastíc pre biomedicínske, biochemické a inžinierske aplikácie | |
| Interactions of nanoparticles with amyloid fibrils: from therapy to nanomaterials | |
| Program: | Bilateral – other |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Annotation: | Nanoparticles represent a powerful platform with a large potential for biomedicine and engineering applications.The formation of amyloid aggregates is unfavorable in vivo as they are associated with the pathogenesis of many human diseases, yet, amyloid fibrils have the potential to be engineered into novel materials. However, there is still little known about the interactions between amyloid fibrils and nanoparticles that can provide new enhanced NPs functions. The project aims to investigate the interaction of amyloid fibrils formed from native globular proteins and nanoparticles to utilize or enhance the NPs applications as catalysts in engineering applications or possible disaggregation agents to treat amyloid-related diseases (Alzheimer´s disease, diabetes mellitus). We will determine the relationship between amyloid fibrils (formed from lysozyme, insulin, and α -lactalbumin) and Au-, Ag- and Pd –nanoparticles with different surface chemistry (size, charge, functionalization). Moreover, we will perform a systematic study of globular proteins\’ propensity to form amyloid fibrils with controlled properties. The proposed objectives will be achieved by combining experimental techniques with computational methods routinely used in respective scientific teams. Moreover, the data about fibrils\’ structural and physico-chemical properties might fill the empty spaces in a big biology puzzle – pathophysiology of amyloid-related diseases. |
| Duration: | 1.1.2022 – 31.12.2023 |
| Stabilita a agregácia globulárnych proteínov v prítomnosti biokompatibilných iónových kvapalín | |
| Stability and aggregation of globular proteins in the presence of biocompatible ionic liquids | |
| Program: | Mobility |
| Project leader: | RNDr. Fedunová Diana, PhD. |
| Duration: | 1.1.2021 – 31.12.2022 |
| CHINMEDAMY – Identifikácia a mechanizmus účinku malých molekúl využívaných v tradičnej čínskej medicíne na liečbu Alzheimerovej choroby | |
| Discovery and Mechanism of Small Molecule Compounds from Traditional Chinese Medicine for treatment of Alzheimer \’s Disease | |
| Program: | Bilateral – other |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Duration: | 1.1.2018 – 31.12.2019 |
| NGP-NET – Neglobulárne proteíny – od sekvencie ku štruktúre, funkcii a aplikácii v molekulárnej fyziopatológii | |
| Non-globular proteins – from sequence to structure, function and application in molecular physiopathology | |
| Program: | COST |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Annotation: | Non-globular proteins (NGPs) encompass different molecular phenomena that defy the traditional sequence-structure-function paradigm. NGPs include intrinsically disordered regions, tandem repeats, aggregating domains, low-complexity sequences and transmembrane domains. Although growing evidence suggests that NGPs are central to many human diseases, functional annotation is very limited. It was recently estimated that close to 40 of all residues in the human proteome lack functional annotation and many of these are NGPs. While a better understanding of NGPs is crucial to fully comprehend human molecular physiopathology, progress has been hampered so far by the lack of a systematic approach to their study.This Action Proposal aims to create a pan-European scientific network of groups that work on NGPs to strengthen, focus and coordinate research in this field. It proposes to develop a novel classification of NGPs by consensus among interested experts that will be showcased on a newly developed web site, along with meetings, training schools and scientific missions on NGP-related topics. |
| Project webpage: | http://www.cost.eu/COST_Actions/bmbs/BM1405 |
| Duration: | 27.7.2015 – 25.3.2019 |
| Účinok malých molekúl a nanočastíc na amyloidnú agregáciu poly/peptidov | |
| Effect of small molecules and nanoparticles on amyloid aggregation of poly/peptides | |
| Program: | Bilateral – other |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Annotation: | This project is aimed at examining the self-assembly of proteins into amyloid aggregates, one of the hallmarks of AD and other amyloidosis. Accordingly, there is a considerable world-wide interest to identify molecular entities that can influence the amyloid aggregation in order to facilitate the drug development for amyloid diseases. The main goals of the project are to estimate the conditions required for promoting protein misfolding, to determine the cytotoxicity of amyloid aggregates, and to identify the compounds (e.g. small molecules and nanoparticles) that are able to inhibit protein aggregation using in vitro and in silico methods. The bilateral collaboration will allow to combine expertise and experience of both partners in the field of protein aggregation and acquire complex data with aid of complementary approaches, leading to a better understanding of amyloid aggregation mechanisms. The use of equipment provided by both institutions will offer a solid background for team members in order to publish their results at conferences and in journals. Moreover, this collaborative research partnership will present an excellent opportunity for both teams’ young members to learn new techniques in the well-equipped laboratories at NTU and SAS and work as an international scientific research group. |
| Duration: | 11.1.2016 – 31.12.2018 |
| ChinherbAD – Využitie multitargetových nízkomolekulových látok z tradičných čínskych bylín pri liečbe Alzheimerovej choroby | |
| The multitarget low molecular compounds from traditional Chinese herbs in treatment of Alzheimer´s disease | |
| Program: | Bilateral – other |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Annotation: | Alzheimer\’s disease (AD) is a devastating neurodegenerative disorder of multifactorial nature characterized by neuroinflammation, decreasing the level of the neurotransmitter acetylcholine as well as formation of amyloid Abeta peptide plaques and neurofibrillary tangles containing abnormally posttranslationally modified tau protein. There is no effective treatment for AD so far and none of the clinically tested drugs have any feasibility to stop, substantially delay or reverse the progressive consequences of this disease. Accordingly, there is a considerable world-wide interest to facilitate the drug development for AD. Recently, the strategy of using the multi-targeted ligands seems to be the most attractive for developing effective therapy for Alzheimer´s disease due to ability of these compounds interacts with multiple targets responsible for the disease pathogenesis. The main goal of this project is to investigate multi-target responsibility of compounds including extracts from traditional Chinese herbs as potential therapeutic agents for AD. Using in vitro, in vivo and in silico methods we will study ability of these compounds to affect the neuroinflammation, to inhibit acetylcholinesterase activity, and amyloid aggregation of Abeta peptide. The bilateral collaboration will allow the both research groups to combine their expertise and experience in the field of pathology of Alzheimer´s disease. The complementary approach allows obtain more complex data leading to suggestion of possible alternatives of therapy against this devastating disease. Moreover, the project will also enable mutual utilization of equipment provided by both institutions. At the same time the young members of project\’s team will have the opportunity to learn new techniques in well-equipped laboratories at SAS and East China University of Science and Technology and also work in the international scientific team. |
| Duration: | 1.1.2016 – 31.12.2017 |
| AMYTOX – Štúdium amyloidogénnych proteínov a ich cytotoxicity | |
| Investigation of the amyloidogenic proteins in relationship with their cytotoxic effect | |
| Program: | Bilateral – other |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Annotation: | The project offers us the possibility to take part into international collaboration with Romanian Scientists concern to amyloid aggregation of proteins. Moreover, the proposal of the project will enable mutual utilization of equipment provided by both institutions. At the same time the young members of Slovakian team will have the opportunity to learn new techniques in well-equipped laboratories at UMF „Carol Davila“ and work in the international scientific team.The topic of the project includes the research of the protein self-assembly into amyloidal aggregates, since this characteristic is one of the hallmarks of multiple severe diseases(Alzheimer’s disease, non-neuropathic amyloidosis). Although multiple studies in the research field of amyloidosis were carry out, the data on the mechanism formation or reverse of the process of the amyloidosis are missing, and the toxicity of amyloid aggregates remains to be clarified. Our attention will be addressed to assess the conditions required for promotion of protein missfolding, to determine the cytotoxic effect of the amyloids, and to identify molecules able to inhibit protein aggregation. The major advantages of the bilateral cooperation will consist in: i) the study could provide a useful model for understanding the pathological protein aggregation and their cytotoxic action; ii) the scientific output of the project could suggest possible alternatives of therapy against devastating diseases, as different types of dementia or non-neuropathic amyloidosis; iii) the experimental data will offer thepossibility to publish our joint results in the international scientific journals; iv) our collaboration could represent a solid base to apply further for EU funding projects. |
| Duration: | 1.1.2013 – 31.12.2014 |
| LYSACELL – Štúdium amyloidnej agregácie lyzozýmu in vitro a analýza vplyvu agregácie na prežívanie buniek | |
| Investigation of the lysozyme amyloid aggregtiion using in vitro assays and analysing its effects on cell viability and proliferation | |
| Program: | Bilateral – other |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Annotation: | The topic of the project includes the research of the protein self-assembly into amyloidal aggregates, since this characteristic is one of the hallmarks of multiple severe diseases. Amyloidosis is a disorder of protein folding in which normally soluble proteins undergo conformational changes and are deposited in an abnormal fibrillar form. For instance, the presence of tau protein deposits is associated with neurodegenerative diseases, like Alzheimer\’s disease and the presence of lysozyme with systemic amyloidosis.One of the objectives of the project is characterization of the conditions leading to protein conformational changes which promote amyloid aggregation. Also, the attention will be focused to investigate the effect of amyloid assemblies (soluble and insoluble) on viability and proliferation of the cells and to analyse their effects on the cell cycle phases and apoptotic processes. The significant spotlight will be given to identify effective molecules or molecular complexes involved in inhibition or destruction of amyloid polymerization and to examine their cytotoxicity. |
| Duration: | 3.1.2011 – 31.12.2012 |
| – | |
| PROtein interactions monitored by multi-parameter Field Effect Transistors | |
| Program: | FP7 |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Duration: | 1.1.2010 – 1.1.2010 |
National
| Iónové kvapaliny a hlboko eutektické zmesi ako modulátory stability a agregácie proteínov | |
| – | |
| Program: | VEGA |
| Project leader: | RNDr. Fedunová Diana, PhD. |
| Duration: | 1.1.2022 – 31.12.2025 |
| Objasnenie počiatočných štádií amyloidnej agregácie proteínov – od mechanizmu k terapii | |
| Unraveling the early events of protein amyloid aggregation – from mechanism to therapy | |
| Program: | VEGA |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Annotation: | Structural changes of poly/peptides leading to the formation of amyloid aggregates are associated with incurablediseases, like Alzheimer\’s disease or diabetes. While the general mechanisms of fibril formation and theircharacterization are well reported, the early events during poly/peptide fibrillation are still unclear. The project isfocused on understanding the early events mechanisms leading to the formation of pre-fibrillar (partially un/foldedintermediates, nuclei, oligomers) and fibrillar amyloid aggregates of selected globular and intrinsically disorderedproteins. Our focus will be the study of the kinetics of pre-fibrillar structures formation, their morphology, andcytotoxicity, under various experimental conditions, and in the presence of selected interacting partners (smallmolecules, nanoparticles). The obtained results will contribute to understanding the early events of amyloidaggregation and identifying the inhibitors with therapeutic potential for amyloid diseases. |
| Duration: | 1.1.2021 – 31.12.2024 |
| NANOVIR – Nanočastice pre riešenie diagnosticko-terapeutických problémov s COVID-19 (NANOVIR) | |
| – | |
| Program: | Štrukturálne fondy EÚ Výskum a inovácie |
| Project leader: | Ing. Závišová Vlasta, PhD. |
| Project webpage: | https://websrv.saske.sk/uef/veda-a-vyskum/projekty-v-ramci-opvai/nanovir/ |
| Duration: | 3.3.2021 – 30.6.2023 |
| BIOVID-19 – Vývoj biomodelov pre zlepšenie hodnotenia účinnosti liekov a látok, ktoré majú potenciál pri liečbe COVID-19 (BIOVID-19) | |
| – | |
| Program: | Štrukturálne fondy EÚ Výskum a inovácie |
| Project leader: | Ing. Koneracká Martina, CSc. |
| Project webpage: | https://websrv.saske.sk/uef/veda-a-vyskum/projekty-v-ramci-opvai/biovid-19/ |
| Duration: | 29.6.2021 – 30.6.2023 |
| MULTIHIT – Multifunkčné inhibítory poly/peptidov spojených s Alzheimerovou chorobou | |
| Multi-target inhibitors of poly/peptides associated with Alzheimer´s disease | |
| Program: | SRDA |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Duration: | 1.7.2019 – 1.6.2023 |
| Nadmolekulárne komplexy proteínov – konformačné prechody, stabilita a agregácia | |
| Supramolecular complexes of proteins – conformational transitions, stability and aggregation | |
| Program: | VEGA |
| Project leader: | RNDr. Fedunová Diana, PhD. |
| Annotation: | Protein aggregation and self-assembly into supramolecular complexes occurs in various biological processes. Fibrillar aggregates – amyloids are hallmark of various diseases. Amyloid fibrils are part of physiological processes in cells and are also tested as novel biomaterials. The project is focused on study of the effect of two classes of cosolvents on amyloid aggregation of structurally different polypeptides – globular lysozyme and intrinsically disordered Aß peptide. The aim of the project is to find the relation between cosolvent properties and their effect on conformation, stability and kinetics of amyloid aggregation and morphology of obtained fibrils.Elucidation of these relations is important for the understanding of the mechanism of amyloid aggregation and can help to design new therapeutics against amyloid-related diseases, for identification of pathological structuralmotifs of fibrils as well as in biotechnological application of fibrils as novel materials. |
| Duration: | 1.1.2018 – 31.12.2021 |
| Samousporiadanie poly/peptidov do amyloidných agregátov – mechanizmus, inhibícia a cytotoxicita | |
| Self-assembly of poly/peptides into amyloid aggregates – mechanism, inhibition and cytotoxicity | |
| Program: | VEGA |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Annotation: | Amyloid supramolecular complexes formed by poly/peptides are the most prevalent naturally occurring self-assembling systems. Formation of such complexes affects function of poly/peptides and is associated with more than 30 serious amyloid-related diseases such as Alzhemer’s disease or diabetes mellitus. The exactmechanism of amyloid self-assembly of poly/peptides is not known yet and no effective treatment of amyloidosis is established. The goal of the project is to study the mechanism of the amyloid aggregation of poly/petides with different native structures and identification of inhibitors of poly/peptide self-assembly since the inhibition of amyloid formation is one of the possible therapeutic approaches against amyloid-related diseases. We will focus on the determination of the correlation between the morphology of amyloid aggregates and their cytotoxicity as well as on the relationship between structure of the effective inhibitors and their anti-amyloid activity. |
| Duration: | 1.1.2017 – 31.12.2020 |
| Štúdium stability a agregácie natívne rozbalených proteínov | |
| Study of the intrinsically disordered protein stability and aggregation | |
| Program: | VEGA |
| Project leader: | RNDr. Fedunová Diana, PhD. |
| Annotation: | Intrinsically disordered proteins (IDPs) – proteins without ordered stable structure at physiological conditions – are of great interest especially due to their connections to neurodegenerative diseases. Alzheimer’s disease is characterized by deposits of amyloid plaques or neurofibrillary tangles, formed by fibrous assemblies of the A-beta or tau proteins. The growing evidences indicate that oligomers are more toxic species than fibrils. Proposed projects is oriented on study of the effect of external conditions (pH, T, ionic strength, hydrophobicity) and various compounds (denaturants, osmolytes and polyanions) on conformation of tau and A-beta proteins andkinetics of their oligomerization. Another goal is to define how properties of oligomers affect the kinetics of ibrillization and morphology of obtained amyloid fibrils. |
| Duration: | 1.1.2014 – 31.12.2017 |
| – | |
| Inhibitors of protein amyloid aggregation | |
| Program: | VEGA |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Annotation: | Amyloid aggregation is on high interest due to its impact on properties of poly/peptides that are arranged into highly organized amyloid aggregates. Amyloids play an important role in serious diseases (type II diabetes, Alzheimer’s diseases) and impose serious restriction in pharmaceutical utilization of proteins. Although multiple studies were carrying out, the data on the mechanism formation or reverse of amyloidosis are missing. The project is devoted to contribute to the understanding of the process of amyloid aggregation and to identify the active substances (small molecules and nanoparticles) that reduce the amyloid self-assembly of proteins providing a basis for the development of drugs for the treatment of amyloid pathology. We will determine the correlation between the properties of active substances and their anti-amyloid activity. We will identify binding sites for the active compounds and suggest the mechanism binding of active molecules using experimental and mathematical methods. |
| Duration: | 1.1.2013 – 31.12.2016 |
| Výpočtové prístupy štúdia štruktúry, zbaľovania a interakcií biopolymérov | |
| Computational approaches to study structure, folding and interactions of biopolymers | |
| Program: | Podpora MVTS z prostriedkov SAV |
| Project leader: | RNDr. Kožár Tibor, CSc. |
| Annotation: | The PI of this research proposal (Dr. Chin-Kun Hu), CoPI of this proposal(Dr. Ming-Chya Wu), and their collaborators (including Dr. Shura Hayryan, and collaborators from Slovakia, Yerevan, Berlin, etc) have developed protein and computation packages SMMP (simple molecular mechanics for proteins), ARVO (to calculate volume and surface of macromolecules, including proteins, DNA, RNA, etc), and CAVE (to detect cavities of macromolecules and calculate surface area and volumes of cavities). The PI and collaborators also developed efficient combination of Wang-Landau Monte Carlo methods and transition matrix Monte-Carlo method for simulating proteins. They have also calculated three-dimensional (3D) structures of a large numbers of microRNA and will establish a website for such 3D structures.. The PI of the collaborative group in Slovakia, Dr. Tibor Kozar (Department of Biophysics, Institute of Experimental Physics, Slovak Academy of Sciences) is an expert on modeling of glycans and glycoproteins. In this proposal, we will continue to improve SMMP, ARVO, CAVE, microRNA molecular dynamics calculations, and will collobrate with Dr. Tibor Kozar’s group to study glycan and glycoproteins and amyloid aggregates. In addition, significant effort will be devoted to interaction studies of ligands with biomacromolecules nucleic acids and proteins with both, small ligands (potential drugs) as well as nanoparticles in order to target amyloid aggregation being this important for diseases (e.g. Alzheimer\’s disease). |
| Duration: | 1.1.2011 – 31.12.2013 |
| Dobudovanie centra pre kooperatívne javy a fázové prechody v nanosystémoch s pespektívou využitia v nano- a biotechnológiách | |
| – | |
| Program: | EU Structural Funds Research & Development |
| Project leader: | doc. RNDr. Kopčanský Peter, CSc. |
| Duration: | 1.4.2010 – 31.3.2013 |
| Amyloidná agregácia proteínov | |
| Amyloid aggregation of proteins | |
| Program: | VEGA |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Annotation: | Amyloid aggregation of proteins is characteristic of several human pathologies termed amyloid diseases (diabetes type II, Alzheimer\’s and prion diseases) and imposes serious restriction in pharmaceutical and biotechnological utilization of proteins. The proposed project is oriented to the characterization of intramolecular and intermolecular interactions of non-native protein conformers leading to self-assembly of molecules into amyloid aggregates with the aim to determine some common mechanisms required for formation of amyloid structures. The significant focus is given to identification of active substances (low molecular compounds, nanoparticles, molecular complexes) effective in reducing of the amount of amyloid aggregates providing a basis for the development of drugs for the treatment of amyloid pathology. |
| Duration: | 1.1.2010 – 31.12.2012 |
| Vývoj tecnologických postupov magnetických kvapalín pre biomedecínske účely | |
| – | |
| Program: | EU Structural Funds Research & Development |
| Project leader: | doc. RNDr. Kopčanský Peter, CSc. |
| Duration: | 1.1.2010 – 30.6.2012 |
| Komplexy biomakromolekúl s nanočasticami | |
| Biomacromolecule complexes with nanoparticles | |
| Program: | VEGA |
| Project leader: | prof. Ing. Antalík Marián, DrSc. |
| Annotation: | Nanoparticles seem to be very perspective objects in the field of biology and medicine. Proposed project isoriented to the investigation of properties of nanoparticles formed by metal atoms and several metal oxides aswell as to the study of their interactions with biological objects on molecular level. The goal of this project is toprepare nanoparticles coated by different molecules bounded by sulfur bridges and to characterize theirproperties also in the complexes with biomacromolecules. We would like to understand the role of the size andshape of basic metal core of nanoparticle with differently modified surface on its interactions withbiomacromolecules. |
| Duration: | 1.1.2009 – 31.12.2011 |
| Agregácia proteínov a identifikácia inhibítorov agregácie | |
| Protein aggregation and identification of aggregation inhibitors | |
| Program: | VEGA |
| Project leader: | doc. RNDr. Gažová Zuzana, DrSc. |
| Annotation: | The project is focused to obtain new knowledge of the aspects of protein misfolding and protein aggregation as the formation of protein deposits is one of the hallmarks of many very serious diseases and seems to be one of the most important problem in biomedicine\’s and biotechnological utilization of proteins. Project deals with investigation of relationship between various conformational states of proteins and their propensity to aggregate. The disease related protein (lysozyme, tau) as well as model protein system (cytochrome c, myoglobin, polyamino acids) will be used for this purpose. The significant focus will be given to identify inhibitors of protein aggregation. We will searching especially for low molecular compounds. |
| Duration: | 1.1.2007 – 31.12.2009 |