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Enzyme-Catalyzed Gel Proteolysis: An Anomalous Diffusion-Controlled Mechanism

G. C. Fadda ^*, D. Lairez ^*, B. Arrio , J.-P. Carton  and V. Larreta-Garde 

^* Laboratoire Léon Brillouin, Commissariat à l'Energie Atomique/Saclay, Gif-sur-Yvette, France; Laboratoire de Photophysique Moléculaire, Université Paris-Sud, Orsay, France; Laboratoire de Physique de l'État Condensé, Commissariat à l'Energie Atomique/Saclay, Gif-sur-Yvette, France; and Équipe de Recherche Relations Matrice Extracellulaire, Université de Cergy-Pontoise, Cergy-Pontoise, France

Correspondence: Address reprint requests to D. Lairez, Tel.: 33-16-908-7231; Fax: 33-16-908-8261; E-mail: lairez{at}cea.fr.

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.

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