Author
R. Vacha
Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.
Biology Disciplines
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2019-2023 · peak 4/yrCo-Author Collaboration Network
10 top collaborators · 11 mutual co-author links9 papers
Recent·Most cited
Valency of Ligand-Receptor Binding from Pair Potentials
W. Morton, R. Vacha, S. Angioletti-Uberti
This paper shows that valency in ligand-receptor interactions varies with nanoparticle curvature, interaction strength, and concentration, and recommends avoiding pair-potentials for accurate modeling.
bioRxiv · Sep 12, 2023Biophysics
Insertases Scramble Lipids: Molecular Simulations of MTCH2
L. Bartos, A. K. Menon, R. Vacha
The paper uses molecular simulations to show MTCH2 functions as a scramblase by reducing lipid transport barriers, similar to VDAC, suggesting insertases with hydrophilic paths may also act as scramblases.
bioRxiv · Aug 14, 2023Biophysics
Counterintuitive Binding of Phosphorylated DEP Domain from Dishevelled Protein to Negatively Charged Membranes
F. L. Falginella, M. Drabinova, V. Bryja, R. Vacha
The paper shows phosphorylation of DEP domain alters electrostatic potential but enhances binding to negatively charged PA-rich membranes through hydrogen bonds and ion-mediated interactions.
bioRxiv · Jan 27, 2023 · PreprintBiophysics
Phospholipids are imported into mitochondria by VDAC, a dimeric beta barrel scramblase
H. Jahn, L. Bartos, G. I. Dearden, J. S. Dittman, J. C. M. Holthuis, R. Vacha, A. K. Menon
The paper identifies VDAC as a phospholipid scramblase that imports lipids into mitochondria through a mechanism distinct from its channel activity.
bioRxiv · Oct 17, 2022Biochemistry
Design guidelines for α-helical peptides that self-assemble into transmembrane barrel pores killing antibiotic-resistant bacteria
R. Deb, I. Kabelka, J. Pribyl, E. Vreeker, G. Maglia, R. Vacha
This study designs α-helical peptides that self-assemble into transmembrane barrel pores, effectively killing antibiotic-resistant bacteria with low human cell toxicity.
bioRxiv · May 9, 2022 · PreprintBiophysics
Effect of helical kink in antimicrobial peptides on membrane pore formation
A. Türkova, I. Kabelka, T. Kralova, L. Sukenik, S. Pokorna, M. Hof, R. Vacha
This study shows that a helical kink in antimicrobial peptides stabilizes toroidal pores and disrupts barrel-stave pores, with kink position affecting pore structure and antimicrobial activity.
bioRxiv · Feb 10, 2020Biophysics
Magainin 2 and PGLa in Bacterial Membrane Mimics II: Membrane Fusion and Sponge Phase Formation
I. Kabelka, M. Pachler, S. Prevost, I. Letofsky-Papst, K. Lohner, G. Pabst, R. Vacha
This paper investigates how magainin 2 and PGLa mixtures interact with bacterial membrane mimics, showing they form fibril-like structures that lead to membrane adhesion, fusion, and sponge phase formation.
bioRxiv · Sep 10, 2019Biophysics
Magainin 2 and PGLa in Bacterial Membrane Mimics I: Peptide-Peptide and Lipid-Peptide Interactions
M. Pachler, I. Kabelka, M.-S. Appavou, K. Lohner, R. Vacha, G. Pabst
This study investigates the synergistic activity of antimicrobial peptides MG2a and PGLa by analyzing their interactions in lipid membranes using experimental and simulation methods.
bioRxiv · Sep 2, 2019Biophysics