Classification of the binding modes in bovine serum albumin using terminally substituted alkane analogues

Kô Takehara, Yuki Morinaga, Shinya Nakashima, Shiro Matsuoka, Hiroshi Kamaya, Issaku Ueda

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Abstract

With the fluorescence probe of 8-anilino-1-naphthalenesulfonate (ANS), the binding modes of terminally substituted alkane analogues (C n X; X = COOH, OH, CHO, NH 3 , CONH 2 ) to bovine serum albumin (BSA) were investigated using a competitive binding technique. The Scatchard plot of the fluorometric titration of BSA with ANS showed that the maximum binding number of ANS, n max , was 3.81, with the binding constant, K bnd , of 1.42 × 10 6 mol -1 dm 3 . The binding modes of C n X to BSA were analyzed based on the fluorometric titration of the ANS and BSA mixture with C n X. C n COOH completely displaced the ANS bound to BSA, whereas C n OH and C n CHO displaced only about 40% of the ANS bound to BSA. In contrast, C n NH 2 and C n CONH 2 displaced very little bound ANS. By comparing these results, we classified the binding modes of C n X to BSA into three types. Two of them are detectable with the ANS fluorescence and the remaining one is not detectable with the fluorescence. 2006

Original languageEnglish
Pages (from-to)1571-1575
Number of pages5
Journalanalytical sciences
Volume22
Issue number12
DOIs
Publication statusPublished - Dec 2006

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All Science Journal Classification (ASJC) codes

  • Analytical Chemistry

Cite this

Takehara, K., Morinaga, Y., Nakashima, S., Matsuoka, S., Kamaya, H., & Ueda, I. (2006). Classification of the binding modes in bovine serum albumin using terminally substituted alkane analogues. analytical sciences, 22(12), 1571-1575. https://doi.org/10.2116/analsci.22.1571