Prof. Dr. Joachim Dzubiella
Profil
Zusammenfassung
Joachim Dzubiella entwickelt theoretische Modelle und Computersimulationen, um zu verstehen, wie Moleküle und Materialien in Lösungen miteinander wechselwirken – insbesondere wie Proteine, Polymere und Nanopartikel sich verhalten. Seine Expertise umfasst die Vorhersage von Adsorption, Katalyse und Phasenübergängen auf molekularer Ebene, was für die Entwicklung von Biomaterialien, intelligenten Polymeren und katalytischen Systemen praktisch relevant ist.
Skills
Stammdaten
Identität, Organisation und Kontakt aus HU-FIS.
Forschungsthemen8
Modellierung von Zelladhaesion mithilfe Weicher-Materie Modellsysteme
Quelle ↗Förderer: Alexander von Humboldt-Stiftung Zeitraum: 05/2013 - 04/2015 Projektleitung: Prof. Dr. Joachim Dzubiella
Molekulardynamische Simulationsstudie über die Lamination von Polycarbonat
Quelle ↗Zeitraum: 04/2016 - 09/2016 Projektleitung: Prof. Dr. Joachim Dzubiella
NW: Stabilitaet halophiler Proteine II
Quelle ↗Förderer: DFG Nachwuchsgruppe Zeitraum: 10/2011 - 07/2013 Projektleitung: Prof. Dr. Joachim Dzubiella
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Publikationen25
Top 25 nach Zitationen — Quelle: OpenAlex (BAAI/bge-m3 embedded für Matching).
Chemical Society Reviews · 1084 Zitationen · DOI
Catalysis by metallic nanoparticles is certainly among the most intensely studied problems in modern nanoscience. However, reliable tests for catalytic performance of such nanoparticles are often poorly defined, which makes comparison and benchmarking rather difficult. We tackle in this tutorial review a subset of well-studied reactions that take place in aqueous phase and for which a comprehensive kinetic analysis is available. Two of these catalytic model reactions are under consideration here, namely the reduction of (i) p-nitrophenol and (ii) hexacyanoferrate (iii), both by borohydride ions. Both reactions take place at the surface of noble metal nanoparticles at room temperature and can be accurately monitored by UV-vis spectroscopy. Moreover, the total surface area of the nanoparticles in solution can be known with high precision and thus can be directly used for the kinetic analysis. Hence, these model reactions represent cases of heterogeneous catalysis that can be modelled with the accuracy typically available for homogeneous catalysis. Both model reactions allow us to discuss a number of important concepts and questions, namely the dependence of catalytic activity on the size of the nanoparticles, electrochemistry of nanoparticles, surface restructuring, the use of carrier systems and the role of diffusion control.
Angewandte Chemie International Edition · 737 Zitationen · DOI
Protein adsorption is considered to be the most important factor of the interaction between polymeric biomaterials and body fluids or tissues. Water-mediated hydrophobic and hydration forces as well as electrostatic interactions are believed to be the major factors of protein adsorption. A systematic analysis of various monolayer systems has resulted in general guidelines, the so-called "Whitesides rules". These concepts have been successfully applied for designing various protein-resistant surfaces and are being studied to expand the understanding of protein-material interactions beyond existing limitations. Theories on the mechanisms of protein adsorption are constantly being improved due to the fast-developing analytical technologies. This Review is aimed at improving these empirical guidelines with regard to present theoretical and analytical advances. Current analytical methods to test mechanistic hypotheses and theories of protein-surface interactions will be discussed. Special focus will be given to state-of-the-art bioinert and biospecific coatings and their applications in biomedicine.
The Journal of Physical Chemistry B · 676 Zitationen · DOI
Ions differ in their ability to salt out proteins from solution as expressed in the lyotropic or Hofmeister series of cations and anions. Since its first formulation in 1888, this series has been invoked in a plethora of effects, going beyond the original salting out/salting in idea to include enzyme activities and the crystallization of proteins, as well as to processes not involving proteins like ion exchange, the surface tension of electrolytes, or bubble coalescence. Although it has been clear that the Hofmeister series is intimately connected to ion hydration in homogeneous and heterogeneous environments and to ion pairing, its molecular origin has not been fully understood. This situation could have been summarized as follows: Many chemists used the Hofmeister series as a mantra to put a label on ion-specific behavior in various environments, rather than to reach a molecular level understanding and, consequently, an ability to predict a particular effect of a given salt ion on proteins in solutions. In this Feature Article we show that the cationic and anionic Hofmeister series can now be rationalized primarily in terms of specific interactions of salt ions with the backbone and charged side chain groups at the protein surface in solution. At the same time, we demonstrate the limitations of separating Hofmeister effects into independent cationic and anionic contributions due to the electroneutrality condition, as well as specific ion pairing, leading to interactions of ions of opposite polarity. Finally, we outline the route beyond Hofmeister chemistry in the direction of understanding specific roles of ions in various biological functionalities, where generic Hofmeister-type interactions can be complemented or even overruled by particular steric arrangements in various ion binding sites.
Kooperationen1
Bestätigte Forscher↔Partner-Paare aus HU-FIS — Gold-Standard-Positive für das Matching.
SFB 951/2: Untersuchung von Strukturbildung in HIOS auf molekularen Skalen mit Hilfe von atomar aufgelösten molekulardynamischen Computersimulationen (TP A01)
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