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Vitali Vogel

Researcher at Goethe University Frankfurt

Publications -  40
Citations -  2278

Vitali Vogel is an academic researcher from Goethe University Frankfurt. The author has contributed to research in topics: Particle size & Nanoparticle. The author has an hindex of 22, co-authored 40 publications receiving 2030 citations.

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Journal ArticleDOI

Physicochemical characterization of protamine-phosphorothioate nanoparticles

TL;DR: Improvements in particle preparation and the physicochemical properties of the complexes prepared are described and the influence of component concentrations, length of the PTO chain and thePTO/protamine weight ratio on particle formation and size, shape and surface charge of the particles were studied in detail.
Book ChapterDOI

Characterization of serum albumin nanoparticles by sedimentation velocity analysis and electron microscopy

TL;DR: The procedure described for the analysis of the size distribution of the HSA nanoparticles may be of significant value for the optimization of the method of preparation.
Journal ArticleDOI

A liver-mimicking MRI phantom for thermal ablation experiments.

TL;DR: The constructed phantom is heat-resistant and MR-compatible and can be used as an alternative to liver tissue in the MR-guided thermal ablation experiments with laser to develop clinical tools for real-time monitoring and controlling the thermal ablated progress in liver.
Journal ArticleDOI

Optimizing novel implant formulations for the prolonged release of biopharmaceuticals using in vitro and in vivo imaging techniques.

TL;DR: A biodegradable implant was developed, based on a combination of nanoencapsulation of protein-heparin complexes, creation of a slow release matrix by freeze-drying, and compression using hyaluronan and methylcellulose, to establish a parenteral dosage form with prolonged release properties.
Journal ArticleDOI

Monitoring of Demasking of Peptide Bonds During Proteolysis by Analysis of the Apparent Spectral Shift of Intrinsic Protein Fluorescence

TL;DR: Demasking of peptide bonds during proteolysis of β-casein and β-lactoglobulin by trypsin was monitored by the measurement of the overall spectral shift of intrinsic protein fluorescence, showing that the fluorescence shift can be attributed to the demasking stage.