Enzyme-catalyzed gel proteolysis: an anomalous diffusion-controlled mechanism.
Enzyme-catalyzed proteolysis of gelatin gels has been studied. We report a gel degradation rate varying as the square of the enzyme concentration. The diffusion motion of enzymes in the gel has been measured by two-photon fluorescence correlation spectroscopy and identified as being anomalously slow. These experimental results are discussed from a theoretical point of view and interpreted in terms of a diffusion-controlled mechanism for the gel degradation. These results make a step toward the understanding of enzyme-catalyzed gel degradation and give new insight on biological processes such as the action of metalloproteinases in the extracellular matrix involved in cellular invasion.
Laboratoire Léon Brillouin, Commissariat à l'Energie Atomique/Saclay, Gif-sur-Yvette, France.
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D002384:Catalysis; D003198:Computer Simulation; D004058:Diffusion; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry; D016326:Extracellular Matrix Proteins / Q000737:chemistry; D005780:Gelatin / Q000737:chemistry*; D006868:Hydrolysis; D046911:Macromolecular Substances; D008956:Models, Chemical; D010447:Peptide Hydrolases / Q000737:chemistry*; D044367:Phase Transition; D011489:Protein Denaturation; D013050:Spectrometry, Fluorescence / Q000379:methods; D013820:Thermolysin / Q000737:chemistry*
D004800:Enzymes, Immobilized; D016326:Extracellular Matrix Proteins; D046911:Macromolecular Substances; D005780:Gelatin; D010447:Peptide Hydrolases; D013820:Thermolysin