Összes szerző

Ilyés Kinga

az alábbi absztraktok szerzői között szerepel:

Bóta Attila
Nanoerythrosome-based promising drug delivery system

Aug 30 - szerda

15:30 – 17:00

II. Poszterszekció

P38

Nanoerythrosome-based promising drug delivery systems

Attila Bóta¹, Judith Mihály¹, Kinga Ilyés¹, Bence Fehér², Tünde Juhász³, András Wacha¹, Heinz Amenitsch⁴ and Zoltán Varga¹

¹Research Centre for Natural Sciences, Biological Nanochemistry Research Group, Budapest

²Laboratory of Self-Organizing Soft Matter, Department of Chemical Engineering and Chemistry, Eindhoven University of Technology, Eindhoven, The Netherlands

³Research Centre for Natural Sciences, Biomolecular Self-assembly Research Group, Budapest

⁴Austrian SAXS beamline@ELETTRA, Are Science Park, Basovizza TS, Trieste, Italy and Inorganic Chemistry, Graz University of Technology, Graz, Austria

Nanoerythrosomes are artificial vesicle-like objects formed from erythrocyte-membranes, named ghosts, by physical processes, such as extrusion or sonication. Phosphatidylcholines (PCs) and sphingomyelins (SMs) are outer membrane constituents, while phosphatidylserines (PSs) and phosphatidylethanolamine (PEs) generally take place on the inner side of the membrane-bilayer. By addition of different artificial lipids, very different size-ranges of nanoerythrosomes can be achieved, therefore proper reference materials and drug delivery systems with adequate surface chemical behaviour can be prepared [1]. The presence of dipalmitoyl-phosphatidylethanolamine (DPPE) results in the formation of larger nanoerythrosomes, while the addition of dipalmitoylphosphatidylcholine (DPPC) induces the formation in a middle-range (140 -160 nm). The presence of the mixture of DPPC - LPC (lysophosphatidylcholine) causes bicelle – micelle type nanoparticles [2]. Here we show that in the complex physic-chemical study, among the different experimental methods (transmission electron-microscopy combined with freeze-fracture (FF-TEM), Microfluidic Resistive Pulse Sensing (MRPS), dynamic light scattering (DLS), the small-angle X-ray scattering (SAXS) turned out to be a powerful tool in the complex physic-chemical study of this drug delivery system.

Acknowledgment

The project was supported by the National Research, Development and Innovation Office of Hungary under grants K131657 (A. Bóta) and K131594 (J. Mihály) and 2018-1.2.1-NKP-2018-00005 under the 2018-1.2.1-NKP funding scheme (A. Bóta, Z. Varga). Z Varga and A. Wacha are supported by the János Bolyai Research Scholarship of the HAS.

References

[1] Deák R, Mihály J, Szigyártó ICS, Beke-Somfai T, Turiák L, Drahos L, Wacha A, Bóta A and Varga Z (2020)  Mat. Sci. and Eng. C 109:110428-110437.

[2] Bóta A, Fehér B, Wacha A, Juhász T, Szabó D, Turiák L, Gaál A, Varga Z, Amenitsch H and Mihály J(2023) J Mol. Liq. 369: 120791-120800.

Tasvilla Sonallya
Systematic investigation and classification of host defence and cell penetrating peptides based on their affinity for interaction with extracellular vesicles

Aug 30 - szerda

09:55 – 10:10

Membránok és membránfehérjék biofizikája

E24

Systematic investigation and classification of host defence and cell penetrating peptides based on their affinity for interaction with extracellular vesicles.

Tasvilla Sonallya^1,2, Imola Cs. Szigyártó¹ , Tünde Juhász¹, Edit I. Buzas^4,5,6 Delaram Khamari ⁴,Kinga Ilyes^2,3 Zoltán Varga³, and Tamás Beke-Somfai^1*

¹Institute of Materials and Environmental Chemistry, Biomolecular Self-assembly Research Group, Research Centre for Natural Sciences, Budapest H-1117, Magyar tudósok körútja 2, Hungary,

²Hevesy György PhD School of Chemistry, ELTE Eötvös Loránd University, Budapest H-1117, Pázmány Péter sétány 1/A, Hungary.

³Institute of Materials and Environmental Chemistry, Biological Nanochemistry Research Group, Research Centre for Natural Sciences, Budapest, H-1117, Magyar tudósok körútja 2, Hungary.

⁴Department of Genetics, Cell and Immunobiology, Semmelweis University, Budapest, Hungary

⁵HCEMM Extracellular Vesicle Research Group, Semmelweis University, Budapest, Hungary

⁶ELKH-SE Immune-Proteogenomics Extracellular Vesicle Research Group, Budapest, Hungary.

Host defence peptides (HDP) are promising biomaterials with antimicrobial and anticancer applications. By disturbing or lysing the cell membrane, they carry out their biological role. These peptides show numerous types of membrane interaction mechanisms i.e., carpet, toroidal pore, and barrel stave. Cell penetrating peptide find application in cargo loading and uptake of small molecules and nanoparticles. The interactive mechanism of these peptides has been studied widely with model membranes however our knowledge with extracellular vesicles (EV) is scarce. There are several aspects where EV – HDP interactions could be relevant, ranging from cooperative presence on infection sites functions to EV cargo loading. Hence, based on their in-depth investigation using biophysical techniques, the binding affinity with extracellular vesicles was studied and categorised as low binding affinity, medium binding affinity and high affinity. This initial categorisation gives further insight into its specific interactive mechanism.

Acknowledgment:

This work was funded by the Ministry of Innovation and Technology of Hungary through the National Research, Development and Innovation Office, financed under the TKP2021-EGA-31, the 2020-1-1-2-PIACI-KFI_2020-00021, 2019-2.1.11-TÉT-2019-00091 and KKP_22 project no. 144180. Support from Eötvös Loránd Research Network, grant no. SA-87/2021 and KEP-5/2021 is also acknowledged. Z.V. was supported by the János Bolyai Research Scholarship of the Hungarian Academy of Sciences.

References

1. Singh, P. et al. Removal and identification of external protein corona members from RBC‐derived extracellular vesicles by surface manipulating antimicrobial peptides. J. Extracell. Biol. 2, (2023).

2. Singh, P. et al. Membrane Active Peptides Remove Surface Adsorbed Protein Corona From Extracellular Vesicles of Red Blood Cells. Front. Chem. 8, (2020).

Varga Zoltán
In vivo Biodistribution of Extracellular Vesicles: Developing Efficient Radiolabeling Techniques

Aug 29 - kedd

14:00 – 14:20

Orvosi biofizika és sugárbiológia

E14

In vivo Biodistribution of Extracellular Vesicles: Developing Efficient Radiolabeling Techniques

Zoltán Varga¹, Kinga Ilyés¹, Dávid Szöllősi², Ildikó Horváth², Domokos Máthé^2,3, Krisztina Németh^4,5, Viola Tamási^4,*, Edit I Buzás^4,5,6, Krisztián Szigeti²

¹ Biological Nanochemistry Research Group, Research Centre for Natural Sciences

² Department of Biophysics and Radiation Biology, Semmelweis University

³ HCMM-SE In Vivo Imaging Advanced Core Facility

⁴ Department of Genetics, Cell- and Immunobiology, Semmelweis University

⁵ ELKH-SE Translational Extracellular Vesicle Research Group

⁶ HCMM-SE Extracellular Vesicle Research Group

^*current affiliation: Department of Molecular Biology, Semmelweis University

The understanding of extracellular vesicle (EV) biodistribution plays an important role in advancing circulating biomarker research. Nuclear imaging techniques like single-photon emission computed tomography (SPECT) hold potential, but the literature on radioisotope labeling of EVs for in vivo studies remains scarce. This presentation explores the evolution of novel radiolabeling methods, focusing on the development and comparative evaluation of various Tc99m radiolabeling strategies.

Our initial method involved the radioisotope labeling of erythrocyte-derived EVs using the Tc99m-tricarbonyl complex [1]. In vivo SPECT/CT biodistribution studies in mice showed that intravenously administered Tc99m-labeled EVs primarily accumulated in the liver and spleen. Our observations suggested good in vivo stability, with a minor fraction of the radioactive label detaching from the EVs. Next, we explored an alternative approach using Tc99m-HYNIC-Duramycin to label cell-derived EVs [2]. Duramycin, a membrane-active peptide, specifically labels EVs, resulting in higher labeling efficiency. Following previous observations, significant uptake of EVs in the liver and the spleen was observed.

The latest experimental focus is on the use of recombinant proteins with His-tag in conjunction with the Tc99m-tricarbonyl complex to label EVs. Preliminary investigations indicate promising superior performance with this method compared to the previous techniques.

This presentation will provide an in-depth comparison of these methods, emphasizing their development process and potential implications for advancing in vivo EV imaging studies. Through a critical evaluation of their advantages and potential limitations, we aim to foster a greater understanding of efficient tracking of EV biodistribution for future research.

References

[1] Varga Z et al. (2016) Cancer Biother. Radiopharm. 31: 168-173.

[2] Németh K et al. (2021) Cell Mol Life Sci 78: 7589–7604