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Biochemical Reactivities of 1,2‐Dehydro‐N‐β‐Alanyldopamine And The Mode of Action of Bioactive 1,2‐Dehydrodopyl Peptides

The objective of the present study is to investigate the biochemical transformations of 1,2‐dehydro‐N‐β‐alanyldopamine (dehydro NBAD), which belongs to the class of bioactive 1,2‐dehydrodopa containing compounds possessing crosslinking and cementing potentials, antioxidant activities, and antibiotic activities. These activities can be ascribed the reactivity of 1,2‐dehydrodopyl unit. To examine their mode of action, we conducted biochemical studies with dehydro NBAD. Tyrosinase oxidized dehydro NBAD to a transient quinone methide imine amide rather than the conventional quinone. This quinone methide rapidly reacted with the starting material forming oligomeric products. Liquid chromatography mass spectrometry analysis of the reaction confirmed the production of dimers and other oligomers. Laccase also oxidized dehydro NBAD to its dimeric products, without producing quinone methide, probably by free radical coupling. Dehydro NBAD is sensitive to alkaline pH and exhibited rapid nonenzymatic oxidation generating oligomers. During this nonenzymatic reaction, facile production of superoxide anions could be observed. Thus dehydro NBAD seems to exhibit its reactivities through the formation of highly reactive quinone methide, and free radicals. These reactions account for the crosslinking as well as antioxidant and antibiotic potentials of dehydrodopa containing units found in a myriad of organisms.