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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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Publication details

The article was received on 06 May 2018, accepted on 24 May 2018 and first published on 24 May 2018


Article type: Paper
DOI: 10.1039/C8OB01055B
Citation: Org. Biomol. Chem., 2018,16, 4320-4324
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    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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