title: Catch bond interaction between cell-surface sulfatase Sulf1 and glycosaminoglycans.
abstract: In biological adhesion, the biophysical mechanism of specific biomolecular interaction can be divided in slip and catch bonds, respectively. Conceptually, slip bonds exhibit a reduced bond lifetime under increased external force and catch bonds, in contrast, exhibit an increased lifetime (for a certain force interval). Since 2003, a handful of biological systems have been identified to display catch bond properties. Upon investigating the specific interaction between the unique hydrophilic domain (HD) of the human cell-surface sulfatase Sulf1 against its physiological glycosaminoglycan (GAG) target heparan sulfate (HS) by single molecule force spectroscopy (SMFS), we found clear evidence of catch bond behavior in this system. The HD, ∼320 amino acids long with dominant positive charge, and its interaction with sulfated GAG-polymers were quantitatively investigated using atomic force microscopy (AFM) based force clamp spectroscopy (FCS) and dynamic force spectroscopy (DFS). In FCS experiments, we found that the catch bond character of HD against GAGs could be attributed to the GAG 6-O-sulfation site whereas only slip bond interaction can be observed in a GAG system where this site is explicitly lacking. We interpreted the binding data within the theoretical framework of a two state two path model, where two slip bonds are coupled forming a double-well interaction potential with an energy difference of ΔE ≈ 9 kBT and a compliance length of Δx ≈ 3.2 nm. Additional DFS experiments support this assumption and allow identification of these two coupled slip-bond states that behave consistently within the Kramers-Bell-Evans model of force-mediated dissociation.
authors: Experimental Biophysics, Physics Faculty, Bielefeld University, Bielefeld, Germany.
authors: Alexander
authors: A
authors: Harder
authors: Experimental Biophysics, Physics Faculty, Bielefeld University, Bielefeld, Germany.
authors: Ann-Kristin
authors: AK
authors: Möller
authors: Biochemistry I, Faculty of Chemistry, Bielefeld University, Bielefeld, Germany.
authors: Fabian
authors: F
authors: Milz
authors: Biochemistry I, Faculty of Chemistry, Bielefeld University, Bielefeld, Germany.
authors: Phillipp
authors: P
authors: Neuhaus
authors: Experimental Biophysics, Physics Faculty, Bielefeld University, Bielefeld, Germany. Electronic address: volker.walhorn@physik.uni-bielefeld.de.
authors: Volker
authors: V
authors: Walhorn
authors: Biochemistry I, Faculty of Chemistry, Bielefeld University, Bielefeld, Germany.
authors: Thomas
authors: T
authors: Dierks
authors: Experimental Biophysics, Physics Faculty, Bielefeld University, Bielefeld, Germany.
authors: Dario
authors: D
authors: Anselmetti
mesh_terms: D006497:Heparan Sulfate / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D011485:Protein Binding; D015238:Sulfotransferases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D006497:Heparan Sulfate; D015238:Sulfotransferases; C470791:SULF1 protein, human