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The H-bond interaction, hydrophobic interaction, electrostatic interaction and binding energies of ACLY with the compounds are as follows: oleocanthal (-6.1 kcal/mol, H-bond interaction: GLY281, SER343, ASN346, GLY664, GLY665), hydrophobic interaction: ALA280, ALA345, electrostatic interaction: no), oleacein (-6.0 kcal/mol, H-bond interaction: GLY309, ASN346, VAL626, GLY664, GLY665), hydrophobic interaction: ALA345, PHE347 electrostatic interaction: no), luteolin (-8.6 kcal/mol), H-bond interaction: SER7, ARG33, ASP60, GLN61, PHE242, GLY243, GLU245, ALA246, hydrophobic interaction: PRO239, PRO240, electrostatic interaction: no), Tyrosol (-5.3 kcal/mol, H-bond interaction: ASN346, PHE347, THR348, hydrophobic interaction: no, electrostatic interaction: no), ezetimibe ( 6.0 kcal/mol, H-bond interaction: GLU250, hydrophobic interaction: PRO241 (Figs

These macromers were then polymerized to form enzymatically degradable PEG hydrogels, with VEGF tethered via a non-degradable PEG linker, resulting in protein release only when the gel is degraded (Figure 2B)