Web of Science: 3 citations, Scopus: 3 citations, Google Scholar: citations
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 Zurich. Institute of Robotics and Intelligent Systems)
Ergeneman, Olga (ETH Zurich. Institute of Robotics and Intelligent Systems)
Pellicer Vilà, Eva M. (Eva Maria) (Universitat Autònoma de Barcelona. Departament de Física)
Sort Viñas, Jordi (Universitat Autònoma de Barcelona. Departament de Física)
Pané i Vidal, Salvador (ETH Zurich. Institute of Robotics and Intelligent Systems)
Nelson, Bradley J. (ETH Zurich. 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)

Date: 2017
Abstract: 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). Unbinding events between FGF-2-heparin complexes were specific and short-lived. Binding between FGF-2 and heparin had strong slip bond characteristics as demonstrated by a decrease of lifetime with tensile force on the complex. Unbinding forces between FGF-2 and heparin were further detailed at different pH as relevant for (patho-) physiological conditions. An acidic pH environment (5. 5) modulated FGF-2-heparin binding as demonstrated by enhanced rupture forces needed to release FGF-2 from the heparin-FGF-2 complex as compared to physiological conditions. This study provides a mechanistic and hypothesis driven model on how molecular forces may impact FGF-2 release and storage during tissue remodeling and repair.
Note: Número d'acord de subvenció EC/FP7/296679
Rights: Tots els drets reservats
Language: Anglès.
Document: article ; recerca ; submittedVersion
Subject: Atomic force spectroscopy ; Extracellular matrix ; Hypoxia ; Isothermal titration calorimetry ; Magnetic actuation
Published in: ACS biomaterials science & engineering, Vol. 3, issue 6 (2017) , p. 1000-1007, ISSN 2373-9878

DOI: 10.1021/acsbiomaterials.6b00723


Preprint
30 p, 759.1 KB

The record appears in these collections:
Research literature > UAB research groups literature > Research Centres and Groups (scientific output) > Experimental sciences > Group of Smart Nanoengineered Materials, Nanomechanics and Nanomagnetism (Gnm3)
Articles > Research articles
Articles > Published articles

 Record created 2018-04-18, last modified 2020-04-25



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