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An inhibition assay of Candida albicans adhesion to gelatin-immobilized membranes was compared with that to intact type I collagen-immobilized membranes using an arginine-glycine-aspartic acid (RGD) containing peptide. As compared with a protein-free membrane, gelatin and collagen significantly enhanced the adherence of C. albicans. The adhesion of the yeast to gelatin was significantly inhibited by the RGD peptides, but not by arginine-glycine-glutamic acid (RGE) peptides. In contrast, attachment to collagen was not inhibited by RGD peptides. These results suggest that the RGD sequence of gelatin and the integrin-like proteins of yeasts may be involved in adherence.

Several recent reports imply the possibility of cariogenicity and periodontal disease linked to denture plaque containing Candida albicans. Adhesion of oral bacteria and Candida species to the extracellular matrix, such as type I collagen, fibronectin and denatured type I collagen, was examined by using adenosine triphosphate (ATP) analysis. The adhesion of C. albicans to intact and denatured type I collagen was significantly greater than those of oral bacteria and other species of Candida. This result suggests that C. albicans possesses the ability to adhere specifically to extracellular matrix, as compared with other Candida species or oral bacteria.

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