Publisher： John Wiley & Sons Inc
E-ISSN： 1439-7641|16|10|2260-2266
ISSN： 1439-4235
Source： CHEMPHYSCHEM, Vol.16, Iss.10, 2015-07, pp. : 2260-2266
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Abstract
AbstractIn this manuscript the X‐ray structures of two potent and known inhibitors of 15‐lipoxygenase, that is, 4‐allyl‐2‐methoxyphenyl‐1‐admantanecarboxylate (1) and allyl‐2‐methoxyphenyl‐1‐cyclohexanecarboxylate (2), are reported. Their solid‐state architectures show that they have a strong ability to establish CH/π and CH⋅⋅⋅HC interactions. For the former interaction, the adamantane or cyclohexane moieties are the CH donors and the electron‐rich methoxyphenyl ring is the π system. For the latter, the CH bonds belong to the aliphatic rings of the inhibitors. Interestingly, the active site of lipoxygenase enzyme family is rich in isoleucine and leucine amino acids that participate in the binding of the unsaturated fatty acid substrate by means of multiple hydrophobic CH⋅⋅⋅HC interactions. By means of theoretical calculations, we analyze the ability of compounds 1 and 2 to establish CH/π and CH⋅⋅⋅HC interactions in the solid state.
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