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Table 2 Effect of soluble (GPO)10 on the binding of pro- or actMMP-2 or pro- or actMMP-9 to CIa

From: Hydroxyproline-containing collagen analogs trigger the release and activation of collagen-sequestered proMMP-2 by competition with prodomain-derived peptide P33-42

  

Binding to CI

  

Without (GPO)10

10× (GPO)10

  

Off rate (s-1)

K d (μM)

Off rate (s-1)

K d (μM)

MMP-2

Pro

0.48

0.07 ± 0.03

0.37

0.10 ± 0.04

 

Act

0.48

0.17 ± 0.05

0.56

0.21 ± 0.15

MMP-9

Pro

0.32

0.12 ± 0.09

0.22

1.22 ± 0.64

 

Act

0.76

0.87 ± 0.39

0.61

1.79 ± 1.81

  1. aMatrix metalloproteinases (MMPs) (100 nM) were passed over collagen type I (CI) immobilized to a sensor chip in the presence or absence of a 10-fold molar excess of Gly-Pro-Hyp triplets (GPO)10. MMP self-activation and activity were prevented by a buffer system consisting of phosphate-buffered saline and 0.05% (vol/vol) Tween 20. K d values and off rates of MMP binding to CI were determined by surface plasmon resonance (SPR) analysis and are shown as mean values ± SD from at least three experiments.