MBFT XXIX. Kongresszus - 2023, Budapest .

Összes szerző

Juhász Tünde

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.

Juhász Tünde Co-assemblies of cationic antimicrobial peptides with anionic small molecules: unique thermophoretic behaviour

Aug 29 - kedd

15:30 – 17:00

I. Poszterszekció

P15

Co-assemblies of cationic antimicrobial peptides with anionic small molecules: unique thermophoretic behaviour

Tünde Juhász¹, Mayra Quemé-Peña¹, Tamás Beke-Somfai¹

¹ Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences

Peptidic supramolecules formed via self- and co-assembly show emerging applications from materials chemistry to biomedicine. Recently we have demonstrated for a couple of cationic, amphiphilic antimicrobial peptides (AMPs) the ability to form co-assemblies with various anionic, aromatic small molecule (SM) binding agents. Their interaction results in modulating their activity in vitro. Herein we addressed interaction systems of four selected AMPs (CM15, Dhvar4, LL-37, and FK-16, coupled to carboxyfluorescein) with four selected SMs (suramin, tartrazine, biliverdin, and bilirubin ditaurate) exploiting the sensitivity of microscale thermophoresis (MST). MST is a solution phase method utilizing the phenomenon of induced thermophoresis where movement of the molecules is monitored via the fluorescence of the target partner. Besides substantial similarities, various scenarios of thermophoretic responses were revealed. Interestingly, negative thermophoresis was frequently observed, and maximal MST responses were typically found not at the highest SM concentrations applied. Findings suggest substantial contributions of charge and hydration effects. Variations in the thermophoretic behaviour could also be attributed to the oligomeric state of the individual components, and the dynamic nature of the association process. Results demonstrate that the MST method is an excellent additional technique for identifying and studying peptidic assemblies.

Acknowledgment

The authors thank for support from LP2016-2, NVKP_16-1-2016-0007, TKP2021-EGA-31, KKP22 144180, SA-87/2021, KEP-5/2021, and 2020-1-1-2-PIACI-KFI_2020-00021.

Pavela Olivér The membrane binding mechanism and oligomerization of the antifungal protein NFAP2 with molecular dynamics simulations

Aug 30 - szerda

10:10 – 10:30

Membránok és membránfehérjék biofizikája

E25

The membrane binding mechanism and oligomerization of the antifungal protein NFAP2 with molecular dynamics simulations

Olivér Pavela¹, Tünde Juhász¹, László Galgóczy^2,3, Tamás Beke-Somfai¹

¹ Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences

² Department of Biotechnology, Faculty of Science and Informatics, University of Szeged

³ Institute of Biochemistry, Biological Research Centre, Eötvös Loránd Research Network

Neosartorya fischeri antifungal protein 2 (NFAP2) is a cysteine-rich, cationic protein with potent anti-Candida activity, which was recently identified [1]. Its antifungal activity includes pore formation in the fungal cell membrane. Here we followed up the previous experimental results with Molecular Dynamics (MD) simulations in order to find out more about the antifungal effect and action mechanism of NFAP2. We used simple lipid bilayer composition models as well as more complex membrane models. An important complex membrane model we built aims to mimick fungal cell membranes. We studied the binding affinity of NFAP2 towards 7 membrane models. We determined which amino acids play crucial role in the binding to the membrane. In addition, we have also investigated the dimerization of NFAP2 with MD simulations. Results indicate that there is a crucial loop region which is expected to play a central role in the initial attachment of NFAP2 to the lipid membranes of the target organism.

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 is also acknowledged.

References

[1] R. Kovács, F. Nagy, Z. Tóth, L. Forgács, L. Tóth, Gy. Váradi, G. K. Tóth, K. Vadászi, A. M. Borman, L. Majoros, L. Galgóczy (2021) The Neosartorya fischeri Antifungal Protein 2 (NFAP2): A New Potential Weapon against Multidrug-Resistant Candida auris Biofilms, Int. J. Mol. Sci., 22: 771.

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:

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).