Table 2 Molecular docking results between Actinidia deliciosa var. Hayward and fibrin.

From: In-vitro and in-silico analyses of the thrombolytic potential of green kiwifruit

Fibrin chain

SASA (Å2)

ΔG

Kd

Cleaved sites (P1,P1’)

Distance (Å)

Aα.1

48.1

−14.5

5.7e-11

Ser50–Cys51

4.6

Aα.2

176.2

−14.1

1.2e-10

Ser166–Arg167

4.9

Aα.3

211.7

−12.5

1.5e-09

Glu172–Val173

4.3

Bβ.1

170.8

−15.4

1.5e-11

Arg346–Gly347

4.2

γ.1

257.8

−12.3

2.1e-09

Leu402–Gly403

4.4

γ.2

114.4

−13.5

2.9e-10

Gly404–Ala405

4.3

  1. SASA: Solvent accessible surface area of the two amino acids at the cleavage site when unbound; ΔG: Gibbs free energy binding; Kd: dissociation constant; P1 and P1’ are the amino acids adjacent to the cleaved peptide bond at the N-terminal and C-terminal sides, respectively.
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