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Issue 23, 2018
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Activation of disulfide bond cleavage triggered by hydrophobization and lipophilization of functionalized dihydroasparagusic acid

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Abstract

Concisely synthesized and functionalized dihydroasparagusic acid (DHAA) derivatives were used to show that the introduction of a hydrophobic functional group dramatically reduced air oxidation activity at the dithiol moieties and dominantly activated the cleavage of S–S bonds in proteins, presumably due to the hydrophobization and lipophilization. Notably, the reaction sites of water-reactive dithiol moieties behaved similarly to hydrophobic and lipophilic functional groups, which suggests impersonation of the reaction site.

Graphical abstract: Activation of disulfide bond cleavage triggered by hydrophobization and lipophilization of functionalized dihydroasparagusic acid

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Supplementary files

Article information


Submitted
06 May 2018
Accepted
24 May 2018
First published
24 May 2018

Org. Biomol. Chem., 2018,16, 4320-4324
Article type
Paper

Activation of disulfide bond cleavage triggered by hydrophobization and lipophilization of functionalized dihydroasparagusic acid

F. Inagaki, M. Momose, N. Maruyama, K. Matsuura, T. Matsunaga and C. Mukai, Org. Biomol. Chem., 2018, 16, 4320
DOI: 10.1039/C8OB01055B

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