Títol:
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Nanomechanics on FGF-2 and heparin reveal slip bond characteristics with pH dependency
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Autor/a:
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Sevim, Semih; Ozer, Sevil; Jones, Gabriel; Wurzel, Joel; Feng, Luying; Fakhraee, Arielle; Shamsudhin, Naveen; Ergeneman, Olga; Pellicer Vilà, Eva Maria; Sort Viñas, Jordi; Pané i Vidal, Salvador; Nelson, Bradley J.; Torun, Hamdi; Lühmann, Tessa
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Abstract:
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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. |
Matèries:
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-Atomic force spectroscopy -Extracellular matrix -Hypoxia -Isothermal titration calorimetry -Magnetic actuation |
Drets:
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open access
Tots els drets reservats.
https://rightsstatements.org/vocab/InC/1.0/ |
Tipus de document:
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Article |
Publicat per:
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Compartir:
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Uri:
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https://ddd.uab.cat/record/189188
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