Title
Alternative model for cathepsin K activation in human dentin
Author
A. Bafail, M. Azizalrahman, T. Vilde, A. Kishen, A. Prakki
Year
2019
Journal
Dental Materials
Abstract
To evaluate the protease activity in dentin matrices subjected to lactic acid (LA) in comparison to polyacrylic acid (PAA) challenge model at cathepsin K (CT-K) optimum pH 5.5 to assess effectiveness of inhibitors in dentin collagen degradation. Dentin disks measuring 0.5 mm prepared from human molars were completely demineralized in 10% H3PO4. Demineralized dentin disks were challenged with 0.1 M LA, 1.1 mM PAA, artificial saliva (AS), or deionized water (C) for 24 h or 7-days. Dentin collagen properties were tested by measurement of %dry mass change, and ultimate tensile strength (UTS). Degradation of dentin type I collagen was measured by telopeptide assays measuring the sub-product release of C-terminal cross-linked telopeptides (ICTP) and C-terminal peptide (CTX) in the incubation media in relation to total protein concentration, which correlates with matrix metalloproteinases (MMPs) and CT-K activities. Gravimetric analysis showed statistically significant difference between C and other groups (p < 0.04) at 24 h. LA specimens showed significantly higher weight loss from 24 h to 7-days (p = 0.02). UTS revealed statistically significant difference between AS and LA at 24 h and 7-days. UTS at 24 h and 7-days for C and AS had significantly higher mean values compared to LA and PAA. Telopeptide assays reported that CTXtp results showed that LA at 24 h had significantly higher mean values compared to C and AS.
Instrument
J-810
Keywords
Circular dichroism, Protein structure, Protein folding, Biochemistry, Materials