7 results match your criteria: "Hungary. kellermayer.miklos@med.semmelweis-univ.hu.[Affiliation]"

The outer membrane (OM) of Gram-negative bacteria is a complex asymmetric bilayer containing lipids, lipopolysaccharides (LPS) and proteins. While it is a mechanical and chemical barrier, it is also the primary surface of bacterial recognition processes that involve infection by and of the bacterium. Uncovering the mechanisms of these biological functions has been hampered by the lack of suitable model systems.

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Single-particle virology.

Biophys Rev

October 2020

Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary.

The development of advanced experimental methodologies, such as optical tweezers, scanning-probe and super-resolved optical microscopies, has led to the evolution of single-molecule biophysics, a field of science that allows direct access to the mechanistic detail of biomolecular structure and function. The extension of single-molecule methods to the investigation of particles such as viruses permits unprecedented insights into the behavior of supramolecular assemblies. Here we address the scope of viral exploration at the level of individual particles.

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The discovery of actin: "to see what everyone else has seen, and to think what nobody has thought".

J Muscle Res Cell Motil

March 2020

Department of Biophysics and Radiation Biology, Faculty of Medicine, Semmelweis University, Tűzoltó str. 37-47, Budapest, IX, 1428, Hungary.

Actin is among the most highly abundant and ubiquitous proteins in eukaryotic cells. The structure, dynamics and functional diversity of actin have continued to mesmerise cell and molecular biologists, biophysicists and physiologists for more than three quarters of a century. The discovery and initial characterization of actin, which took place in the laboratory of Albert Szent-Györgyi by Ilona Banga and Brúnó F.

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The objective of the study was to develop baicalin loaded liquid self-nanoemulsifying drug delivery systems (BSNEDDS) and to characterize them by physicochemical methods in order to optimize the composition and quality attributes. Atomic force microscopy (AFM) was utilized to evaluate the morphological characteristics and size distribution of reconstituted nanoemulsion droplets with a new sample preparation method for the elucidation of individual nanodroplets without any signs of coalescence. Response surface methodology and desirability approach was used to select the optimized composition related to droplet size, zeta-potential, polydispersity index (PDI), and turbidity characteristics.

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Temperature-Dependent Nanomechanics and Topography of Bacteriophage T7.

J Virol

October 2018

Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary

Viruses are nanoscale infectious agents which may be inactivated by heat treatment. The global molecular mechanisms of virus inactivation and the thermally induced structural changes in viruses are not fully understood. In this study, we measured the heat-induced changes in the properties of T7 bacteriophage particles exposed to a two-stage (65°C and 80°C) thermal effect, by using atomic force microscopy (AFM)-based nanomechanical and topographical measurements.

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Forced phage uncorking: viral DNA ejection triggered by a mechanically sensitive switch.

Nanoscale

January 2018

Department of Biophysics and Radiation Biology, Semmelweis University, Tűzoltó u. 37-47, Budapest H-1094, Hungary.

The foremost event of bacteriophage infection is the ejection of genomic material into the host bacterium after virus binding to surface receptor sites. How ejection is triggered is yet unknown. Here we show, in single mature T7 phage particles, that tapping the capsid wall with an oscillating atomic-force-microscope cantilever triggers rapid DNA ejection via the tail complex.

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Stepwise reversible nanomechanical buckling in a viral capsid.

Nanoscale

January 2017

Department of Biophysics and Radiation Biology, Semmelweis University, Tűzoltó u. 37-47., Budapest H-1094, Hungary. and MTA-SE Molecular Biophysics Research Group, Semmelweis University, Tűzoltó u. 37-47., Budapest H-1094, Hungary.

Viruses are nanoscale infectious agents constructed of a proteinaceous capsid that protects the packaged genomic material. Nanoindentation experiments using atomic force microscopy have, in recent years, provided unprecedented insight into the elastic properties, structural stability and maturation-dependent mechanical changes in viruses. However, the dynamics of capsid behavior are still unresolved.

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