Studies on collagen-tannic acid-collagenase ternary system: Inhibition of collagenase against collagenolytic degradation of extracellular matrix component of collagen

Figures & data

Figure 1.  Canonical surface of energy minimized structure of tannic acid (TA, Penta-m-digalloyl-glucose).

Figure 2.  A schematic representation of interaction of collagen with phenolic group of TA leading to polymerization, complex formation.

Table 1.  Michaelis–Menten parameters for ChC hydrolysis of FALGPA at 25°C, pH 7.5 in the presence of varying concentrations of TA.

Nature of treatment	Inhibitor (µM)	Km (mM)	Vmax (mmol s^−1)	Type of inhibition	Ki (µM)
Control	—	0.555	0.2439
	10	0.625
	20	0.714
TA	40	0.833	0.2439	Competitive	20
	80	1.666
	160	3.333

Figure 3.  Lineweaver–Burk plots of FALGPA hydrolysis by ChC in the presence of TA. Assays were performed in Tricine buffer pH 7.5, with varying concentrations FALGPA (0.1–1.6 mM) and TA.

Figure 4.  This figure is focused on the (A) catalytic site of ChC and (B) TA binding to ChC active site.