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Table 3 Effect of thermostability and Hyp content of collagen analogs on the binding kinetics of pro- or actMMP-2 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

  K d for binding to CI (in nM) in the presence of 10-fold molar excess
  - (GPP)10 (POG)5 (GPO)10
ProMMP-2 7.1 ± 0.1 42.1 ± 39.1 155.5 ± 40.3 155.5 ± 50.2
ActMMP-2 250.0 ± 30.0 n.d. n.d. 2,710.0 ± 90.0
  1. aPro- or actMMP-2 (100 nM) was passed over collagen type I (CI) immobilized to a sensor chip in the presence or absence of 10-fold molar excesses of (GPP)10, (POG)5, or (GPO)10. Reagents were dissolved in matrix metalloproteinase (MMP) activity buffer, and MMP-2 activity was specifically blocked by 1 μM Ro 28-2653. K d values of MMP-2 binding to CI were determined by surface plasmon resonance (SPR) analysis and are shown as mean values ± SD from at least three experiments. Hyp, hydroxyproline; GPP, Gly-Pro-Pro; GPO, Gly-Pro-Hyp triplets; n.d., not determined.