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30 p, 759.1 KB Nanomechanics on FGF-2 and heparin reveal slip bond characteristics with pH dependency / Sevim, Semih (Bogazici University. Department of Electrical and Electronics Engineering) ; Ozer, Sevil (Bogazici University. Department of Electrical and Electronics Engineering) ; Jones, Gabriel (Universität Würzburg. Institute of Pharmacy and Food Chemistry) ; Wurzel, Joel (Universität Würzburg. Institute of Pharmacy and Food Chemistry) ; Feng, Luying (Bogazici University. Department of Electrical and Electronics Engineering) ; Fakhraee, Arielle (Aeon Scientific AG) ; Shamsudhin, Naveen (ETH Zürich. Institute of Robotics and Intelligent Systems) ; Ergeneman, Olga (ETH Zürich. Institute of Robotics and Intelligent Systems) ; Pellicer Vilà, Eva Maria (Universitat Autònoma de Barcelona. Departament de Física) ; Sort Viñas, Jordi (Universitat Autònoma de Barcelona. Departament de Física) ; Pané i Vidal, Salvador (ETH Zürich. Institute of Robotics and Intelligent Systems) ; Nelson, Bradley J. (ETH Zürich. Institute of Robotics and Intelligent Systems) ; Torun, Hamdi (Bogazici University. Department of Electrical and Electronics Engineering) ; Lühmann, Tessa (Universität Würzburg. Institute of Pharmacy and Food Chemistry)
Fibroblast growth factor 2 (FGF-2), an important paracrine growth factor, binds electrostatically with low micromolar affinity to heparan sulfates present on extracellular matrix proteins. A single molecular analysis served as a basis to decipher the nanomechanical mechanism of the interaction between FGF-2 and the heparan sulfate surrogate, heparin, with a modular atomic force microscope (AFM) design combining magnetic actuators with force measurements at the low force regime (1 × 10¹ to 1 × 10⁴ pN/s). [...]
2017 - 10.1021/acsbiomaterials.6b00723
ACS biomaterials science & engineering, Vol. 3, issue 6 (2017) , p. 1000-1007  
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