Philipp Baaske

Philipp Baaske

Metropolregion München
16.262 Follower:innen 500+ Kontakte

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I come from a family of craftsmen and grew up in a small village in the north of Bavaria.…

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Berufserfahrung

  • NanoTemper Technologies GmbH Grafik

    NanoTemper Technologies GmbH

    München und Umgebung, Deutschland

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    Metropolregion München

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    Paris, Île-de-France, Frankreich

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    München, Bayern, Deutschland

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    Bonn, Nordrhein-Westfalen, Deutschland

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    München und Umgebung, Deutschland

Ausbildung

Ehrenamt

  • Creative Destruction Lab Grafik

    Mentor

    Creative Destruction Lab

    –Heute 2 Jahre 2 Monate

    Science and Technology

    https://creativedestructionlab.com/mentors/philipp-baaske/
    Creative Destruction Lab (CDL) is a nonprofit organization that delivers an objectives-based program for massively scalable, seed-stage, science- and technology-based companies.

  • btS – Life Sciences Studierendeninitiative e.V. Grafik

    Alumnus

    btS – Life Sciences Studierendeninitiative e.V.

    –Heute 21 Jahre 9 Monate

    Science and Technology

Veröffentlichungen

  • Protein Sizing with Differential Dynamic Microscopy

    Introduced more than 50 years ago, dynamic light scattering (DLS) is routinely used to determine the size distribution of colloidal suspensions as well as of macromolecules in solution, such as proteins, nucleic acids, and their complexes. More recently, differential dynamic microscopy (DDM) has been proposed as a way to perform DLS experiments with a microscope, with much less stringent constraints in terms of cleanliness of the optical surfaces but a potentially lower sensitivity due to the…

    Introduced more than 50 years ago, dynamic light scattering (DLS) is routinely used to determine the size distribution of colloidal suspensions as well as of macromolecules in solution, such as proteins, nucleic acids, and their complexes. More recently, differential dynamic microscopy (DDM) has been proposed as a way to perform DLS experiments with a microscope, with much less stringent constraints in terms of cleanliness of the optical surfaces but a potentially lower sensitivity due to the use of camera-based detectors. In this work, we push bright-field DDM beyond known limits and show it to be sufficiently sensitive to size small macromolecules in diluted solutions. By considering solutions of three different proteins (bovine serum albumin, lysozyme, and pepsin), we accurately determine the diffusion coefficient and hydrodynamic radius of both single proteins and small protein aggregates down to concentrations of a few milligrams per milliliter. In addition, we present preliminary results showing an unexplored potential for the determination of virial coefficients. Our results are in excellent agreement with those obtained in parallel with a state-of-the-art commercial DLS setup, showing that DDM represents a valuable alternative for rapid, label-free protein sizing with an optical microscope.

    Andere Autor:innen
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  • A New Spectral Shift-Based Method to Characterize Molecular Interactions

    ASSAY and Drug Development Technologies

    There are many fluorescence-based applications that can be used to characterize molecular interactions. However, available methods often depend on site-specific labeling techniques or binding-induced changes in conformation or size of the probed target molecule. To overcome these limitations, we applied a ratiometric dual-emission approach that quantifies ligand-induced spectral shifts with sub-nanometer sensitivity. The use of environment-sensitive near-infrared dyes with the method we…

    There are many fluorescence-based applications that can be used to characterize molecular interactions. However, available methods often depend on site-specific labeling techniques or binding-induced changes in conformation or size of the probed target molecule. To overcome these limitations, we applied a ratiometric dual-emission approach that quantifies ligand-induced spectral shifts with sub-nanometer sensitivity. The use of environment-sensitive near-infrared dyes with the method we describe enables affinity measurements and thermodynamic characterization without the explicit need for site-specific labeling or ligand-induced conformational changes. We demonstrate that in-solution spectral shift measurements enable precise characterization of molecular interactions for a variety of biomolecules, including proteins, antibodies, and nucleic acids. Thereby, the described method is not limited to a subset of molecules since even the most challenging samples of research and drug discovery projects like membrane proteins and intrinsically disordered proteins can be analyzed.

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  • An Automated Microscale Thermophoresis Screening Approach for Fragment-Based Lead Discovery

    Journal of Biomolecular Screening

    Fragment-based lead discovery has proved to be an effective alternative to high-throughput screenings in identifying chemical matter that can be developed into robust lead compounds. The search for optimal combinations of biophysical techniques that can correctly and efficiently identify and quantify binding can be challenging due to the physicochemical properties of fragments. In order to minimize the time and costs of screening, optimal combinations of biophysical techniques with maximal…

    Fragment-based lead discovery has proved to be an effective alternative to high-throughput screenings in identifying chemical matter that can be developed into robust lead compounds. The search for optimal combinations of biophysical techniques that can correctly and efficiently identify and quantify binding can be challenging due to the physicochemical properties of fragments. In order to minimize the time and costs of screening, optimal combinations of biophysical techniques with maximal information content, sensitivity, and robustness are needed. Here we describe an approach utilizing automated microscale thermophoresis (MST) affinity screening to identify fragments active against MEK1 kinase. MST identified multiple hits that were confirmed by X-ray crystallography but not detected by orthogonal methods. Furthermore, MST also provided information about ligand-induced aggregation and protein denaturation. The technique delivered a large number of binders while reducing experimentation time and sample consumption, demonstrating the potential of MST to execute and maximize the efficacy of fragment screening campaigns.

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  • MicroScale Thermophoresis: Interaction analysis and beyond

    Journal of Molecular Structure

    MicroScale Thermophoresis (MST) is a powerful technique to quantify biomolecular interactions. It is based on thermophoresis, the directed movement of molecules in a temperature gradient, which strongly depends on a variety of molecular properties such as size, charge, hydration shell or conformation. Thus, this technique is highly sensitive to virtually any change in molecular properties, allowing for a precise quantification of molecular events independent of the size or nature of the…

    MicroScale Thermophoresis (MST) is a powerful technique to quantify biomolecular interactions. It is based on thermophoresis, the directed movement of molecules in a temperature gradient, which strongly depends on a variety of molecular properties such as size, charge, hydration shell or conformation. Thus, this technique is highly sensitive to virtually any change in molecular properties, allowing for a precise quantification of molecular events independent of the size or nature of the investigated specimen.

    During a MST experiment, a temperature gradient is induced by an infrared laser. The directed movement of molecules through the temperature gradient is detected and quantified using either covalently attached or intrinsic fluorophores. By combining the precision of fluorescence detection with the variability and sensitivity of thermophoresis, MST provides a flexible, robust and fast way to dissect molecular interactions.

    In this review, we present recent progress and developments in MST technology and focus on MST applications beyond standard biomolecular interaction studies. By using different model systems, we introduce alternative MST applications – such as determination of binding stoichiometries and binding modes, analysis of protein unfolding, thermodynamics and enzyme kinetics. In addition, wedemonstrate the capability of MST to quantify high-affinity interactions with dissociation constants (Kds) in the low picomolar (pM) range as well as protein-protein interactions in pure mammalian cell lysates.

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  • Structure and function analyses of the purified GPCR human vomeronasal type 1 receptor 1

    SCIENTIFIC REPORTS

    The vomeronasal system is one of several fine-tuned scent-detecting signaling systems in mammals. However, despite significant efforts, how these receptors detect scent remains an enigma. One reason is the lack of sufficient purified receptors to perform detailed biochemical, biophysical and structural analyses. Here we report the ability to express and purify milligrams of purified, functional human vomeronasal receptor hVN1R1. Circular dichroism showed that purified hVN1R1 had an…

    The vomeronasal system is one of several fine-tuned scent-detecting signaling systems in mammals. However, despite significant efforts, how these receptors detect scent remains an enigma. One reason is the lack of sufficient purified receptors to perform detailed biochemical, biophysical and structural analyses. Here we report the ability to express and purify milligrams of purified, functional human vomeronasal receptor hVN1R1. Circular dichroism showed that purified hVN1R1 had an alpha-helical structure, similar to that of other GPCRs. Microscale thermophoresis showed that hVN1R1 bound its known ligand myrtenal with an EC50 ∼1 µM. This expression system can enable structural and functional analyses towards understanding how mammalian scent detection works.

    Andere Autor:innen
    • Karolina Corin
    • Shuguang Zhang
    • Stefan Duhr
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  • Molecular Interaction Studies Using Microscale Thermophoresis

    ASSAY and Drug Development Technologies

    The use of infrared laser sources for creation of localized temperature fields has opened new possibilities for basic research and drug discovery. A recently developed technology, Microscale Thermophoresis (MST), uses this temperature field to perform biomolecular interaction studies. Thermophoresis, the motion of molecules in temperature fields, is very sensitive to changes in size, charge, and solvation shell of a molecule and thus suited for bioanalytics. This review focuses on the…

    The use of infrared laser sources for creation of localized temperature fields has opened new possibilities for basic research and drug discovery. A recently developed technology, Microscale Thermophoresis (MST), uses this temperature field to perform biomolecular interaction studies. Thermophoresis, the motion of molecules in temperature fields, is very sensitive to changes in size, charge, and solvation shell of a molecule and thus suited for bioanalytics. This review focuses on the theoretical background of MST and gives a detailed overview on various applications to demonstrate the broad applicability. Experiments range from the quantification of the affinity of low-molecular-weight binders using fluorescently labeled proteins, to interactions between macromolecules and multi-component complexes like receptor containing liposomes. Information regarding experiment and experimental setup is based on the Monolith NT.115 instrument (NanoTemper Technologies GmbH)

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  • Protein-binding assays in biological liquids using microscale thermophoresis

    Nature Communications

    Protein interactions inside the human body are expected to differ from the situation in vitro. This is crucial when investigating protein functions or developing new drugs. In this study, we present a sample-efficient, free-solution method, termed microscale thermophoresis, that is capable of analysing interactions of proteins or small molecules in biological liquids such as blood serum or cell lysate. The technique is based on the thermophoresis of molecules, which provides information about…

    Protein interactions inside the human body are expected to differ from the situation in vitro. This is crucial when investigating protein functions or developing new drugs. In this study, we present a sample-efficient, free-solution method, termed microscale thermophoresis, that is capable of analysing interactions of proteins or small molecules in biological liquids such as blood serum or cell lysate. The technique is based on the thermophoresis of molecules, which provides information about molecule size, charge and hydration shell. We validated the method using immunologically relevant systems including human interferon gamma and the interaction of calmodulin with calcium. The affinity of the small-molecule inhibitor quercetin to its kinase PKA was determined in buffer and human serum, revealing a 400-fold reduced affinity in serum. This information about the influence of the biological matrix may allow to make more reliable conclusions on protein functionality, and may facilitate more efficient drug development.

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  • Optical Thermophoresis for Quantifying the Buffer Dependence of Aptamer Binding

    Angewandte Chemie International Edition

    Some like it hot: A robust and fast method for characterizing aptamers relies on the distinct thermophoretic movements of molecules in microscopic temperature gradients (see diagram). The binding properties of proteins and even small molecules can be measured within seconds, and less than 1 μL of sample is required. Notably, the technique works well in complex liquids such as human serum.

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  • Biophysical Characterization of Laforin-Carbohydrate Interaction

    Biochemical Journal (Accepted for publication)

    Laforin is a human dual-specificity phosphatase involved in glycogen metabolism regulation containing a carbohydrate binding module (CBM). Mutations in the gene coding for laforin are responsible for the development of Lafora disease, a progressive fatal myoclonus epilepsy with early onset, characterized by the intracellular deposition of abnormally branched, hyper phosphorylated insoluble glycogen-like polymers, called Lafora bodies. Despite the known importance of the CBM domain of laforin in…

    Laforin is a human dual-specificity phosphatase involved in glycogen metabolism regulation containing a carbohydrate binding module (CBM). Mutations in the gene coding for laforin are responsible for the development of Lafora disease, a progressive fatal myoclonus epilepsy with early onset, characterized by the intracellular deposition of abnormally branched, hyper phosphorylated insoluble glycogen-like polymers, called Lafora bodies. Despite the known importance of the CBM domain of laforin in the regulation of glycogen metabolism, the molecular mechanism of laforin-glycogen interaction is still poorly understood. Recently, the structure of laforin with bound maltohexaose was determined, and despite the importance of such breakthrough, some molecular interaction details remained missing. We herein report a thorough biophysical characterization of laforin-carbohydrate interaction using soluble glycans. We demonstrated an increased preference of laforin for the interaction with glycans with higher order of polymerization and confirmed the importance of tryptophan residues for glycan interaction. Moreover, and in line with what has been described for other CBMs and lectins, our results confirmed that laforin-glycan interactions occur with a favorable enthalpic contribution counterbalanced by an unfavorable entropic contribution. The analysis of laforin-glycan interaction through the glycan side by STD NMR has shown that the CBM binding site can accommodate between 5 and 6 sugar units, which is in line with the recently obtained crystal structure of laforin. Overall, the work here presented complements the structural characterization of laforin, and sheds light on the molecular mechanism of laforin glycan interaction, which is a pivotal requisite to understand the physiological and pathological roles of laforin.

    Andere Autor:innen

Auszeichnungen/Preise

  • TOP100 Innovator of the year 2021

    https://www.top100.de/die-top-innovatoren/2021/nanotemper-technologies-gmbh-2.html

    Lebenswichtige Impfstoffe, hochwirksame Chemotherapeutika oder Medikamente zur Behandlung genetisch bedingter Krankheiten müssen präzise auf ihre Wirkung, ihre Haltbarkeit und ihre Transport- und Lagerfähigkeit geprüft werden. Solche Substanzen bestehen aus winzigen Molekülen, die weder mit dem bloßen Auge noch unter dem Mikroskop erkennbar sind. NanoTemper versteht sich mit ihrem Portfolio auf der Basis weltweit patentierter optischer Messverfahren als Nummer eins in der…

    Lebenswichtige Impfstoffe, hochwirksame Chemotherapeutika oder Medikamente zur Behandlung genetisch bedingter Krankheiten müssen präzise auf ihre Wirkung, ihre Haltbarkeit und ihre Transport- und Lagerfähigkeit geprüft werden. Solche Substanzen bestehen aus winzigen Molekülen, die weder mit dem bloßen Auge noch unter dem Mikroskop erkennbar sind. NanoTemper versteht sich mit ihrem Portfolio auf der Basis weltweit patentierter optischer Messverfahren als Nummer eins in der Labortechnik.

    Die Gründer Dr. Philipp Baaske und Dr. Stefan Duhr entwickelten ihre Methode zur Messung von Biotherapeutika an der Münchener Ludwig-Maximilians-Universität. „Präparate aus 3-D-strukturierten Biomolekülen sind sehr komplex und empfindlich, man darf sie nicht berühren“, erläutert Dr. Philipp Baaske. „Unser Verfahren lässt unter anderem eindeutig erkennen, ob sie im Körper an der richtigen Stelle anbinden und ob sie die gewünschte Wirkung erzielen.“ 2008 ins Leben gerufen, vermarktet NanoTemper heute weltweit selbst entwickelte und gefertigte Messgeräte sowie Software, Applikationen und Verbrauchsmittel wie spezielle Glaskapillaren. Zu den Kunden zählen Global Player der Pharmaindustrie, innovative Biotechunternehmen und renommierte Forschungseinrichtungen wie das Max-Planck-Institut. Rund 90 % der Erzeugnisse gehen in den Export.
    Weltweit sind in dem Unternehmen mit Stammsitz in München 170 Beschäftigte aus 29 Nationen tätig, ein Viertel davon in Forschung und Entwicklung. Frauen stellen die Hälfte des Führungsteams. Den Biologen, Chemikern, Physikern, Programmierern und Ingenieuren im F&E-Bereich gewährt das Top-Management einen hohen Vertrauensvorschuss und maximalen Freiraum. „Hier finden sich starke, kulturell sehr unterschiedlich geprägte Persönlichkeiten“, betont Dr. Stefan Duhr. „Wir zwingen ihnen Abläufe nicht auf, sondern passen sie so weit wie möglich den Kenntnissen und Fähigkeiten unserer Mitarbeitenden an. So sind alle kreativ und motiviert bei der Sache.“

  • Berufung in den Bundeswirtschaftssenat

    Bundesverband mittelständischer Wirtschaft

    https://www.bvmw.de/sektionen/wirtschaftssenat/bundeswirtschaftssenat/

  • TOP100 Innovator des Jahres 2018

    TOP 100 - https://www.top100.de/

    https://www.top100.de/die-top-innovatoren/2018/nanotemper-technologies-gmbh-1.html

  • TOP100 Innovator des Jahres 2017

    TOP100

    https://www.top100.de/die-top-innovatoren/2017/nanotemper-technologies-gmbh.html

  • One of Germany's most promising talents Top 40 below the age of 40 - category: entrepeneur

    Capital

    Die Zeitschrift Capital hat das Projekt 2007 ins Leben gerufen und kürt seither jedes Jahr die herausragenden Talente des Landes unter 40 Jahren. Ausgezeichnet werden jeweils 40 junge Menschen in den vier Kategorien „Unternehmer“, „Manager“, „Politik und Staat“, „Gesellschaft und Wissenschaft“. Die Redaktion befragt dazu Manager, Politiker, Headhunter und Berater sowie die Ausgezeichneten der Vorjahre, aus deren Vorschlägen in internen Juryrunden 160 Preisträger ausgewählt werden.

  • Deutscher Gründerpreis 2014 - Kategorie Aufsteiger

    Deutscher Gründerpreis

    http://www.deutscher-gruenderpreis.de/preistraeger/2014/nanotemper-technologies/

  • Deutscher Innovationspreis

    Wirtschafts Woche

    https://www.wiwo.de/technologie/forschung/innovationspreis-auf-der-jagd-nach-neuen-medikamenten/6333942.html

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  • Deutsch

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