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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

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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)

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The skin has a particularly complicated connection with the gut, but the underlying mechanism is still completely understood, and this phenomenon is at least partially attributed to the disruption of the intestinal barrier (Kim et al., 2014