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. 2020 Jun 18;9(6):533. doi: 10.3390/antiox9060533

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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(a) Putative interactions between apigenin and MMP-12 (PDB: 3F17). Free energy of binding (ΔG) and affinity (Ki) are −8.3 kcal/mol and 0.8 µM, respectively. (b) Putative interactions between isovitexin and MMP-12 (PDB: 3F17). Free energy of binding (ΔG) and affinity (Ki) are −8.8 kcal/mol and 0.4 µM, respectively. (c) Putative interactions between luteolin and MMP-12 (PDB: 3F17). Free energy of binding (ΔG) and affinity (Ki) are −8.7 kcal/mol and 0.4 µM, respectively. (d) Putative interactions between quercetin and MMP-12 (PDB: 3F17). Free energy of binding (ΔG) and affinity (Ki) are −8.7 kcal/mol and 0.4 µM, respectively. (e) Putative interactions between vitexin and MMP-12 (PDB: 3F17). Free energy of binding (ΔG) and affinity (Ki) are −8.8 kcal/mol and 0.3 µM, respectively. (f) Putative interactions between apigenin and lanosterol-14-alpha demethylase (PDB: 4LXJ). Free energy of binding (ΔG) and affinity (Ki) are −8.8 kcal/mol and 0.4 µM, respectively.

(a) Putative interactions between apigenin and MMP-12 (PDB: 3F17). Free energy of binding (ΔG) and affinity (Ki) are −8.3 kcal/mol and 0.8 µM, respectively. (b) Putative interactions between isovitexin and MMP-12 (PDB: 3F17). Free energy of binding (ΔG) and affinity (Ki) are −8.8 kcal/mol and 0.4 µM, respectively. (c) Putative interactions between luteolin and MMP-12 (PDB: 3F17). Free energy of binding (ΔG) and affinity (Ki) are −8.7 kcal/mol and 0.4 µM, respectively. (d) Putative interactions between quercetin and MMP-12 (PDB: 3F17). Free energy of binding (ΔG) and affinity (Ki) are −8.7 kcal/mol and 0.4 µM, respectively. (e) Putative interactions between vitexin and MMP-12 (PDB: 3F17). Free energy of binding (ΔG) and affinity (Ki) are −8.8 kcal/mol and 0.3 µM, respectively. (f) Putative interactions between apigenin and lanosterol-14-alpha demethylase (PDB: 4LXJ). Free energy of binding (ΔG) and affinity (Ki) are −8.8 kcal/mol and 0.4 µM, respectively.