Explaining the highly enantiomeric photocyclodimerization of 2-anthracenecarboxylate bound to human serum albumin using time-resolved anisotropy studies

Denis Fuentealba; Hanako Kato; Masaki Nishijima; Gaku Fukuhara; Tadashi Mori; Yoshihisa Inoue; Cornelia Bohne

doi:10.1021/ja3081555

Explaining the highly enantiomeric photocyclodimerization of 2-anthracenecarboxylate bound to human serum albumin using time-resolved anisotropy studies

Denis Fuentealba, Hanako Kato, Masaki Nishijima, Gaku Fukuhara, Tadashi Mori, Yoshihisa Inoue, Cornelia Bohne

Research output: Contribution to journal › Article › peer-review

58 Citations (Scopus)

Abstract

The mechanism for the high enantiomeric excess (ee) (80-90%) observed in the photocyclodimerization of 2-anthracenecarboxylate (AC) in the chiral binding sites of human serum albumin (HSA) was studied using fluorescence anisotropy. A long rotational correlation time of 36 ns was observed for the excited states of the ACs bound to the HSA site responsible for the high ee, suggesting that the ACs have restricted rotational mobility in this site. The ACs in this site have the same prochiral face protected by the protein, and this protection is responsible for the high ee observed. These insights provide a strategy for the rational design of supramolecular photochirogenic systems.

Original language	English
Pages (from-to)	203-209
Number of pages	7
Journal	Journal of the American Chemical Society
Volume	135
Issue number	1
DOIs	https://doi.org/10.1021/ja3081555
Publication status	Published - 2013 Jan 9
Externally published	Yes

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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abstract = "The mechanism for the high enantiomeric excess (ee) (80-90%) observed in the photocyclodimerization of 2-anthracenecarboxylate (AC) in the chiral binding sites of human serum albumin (HSA) was studied using fluorescence anisotropy. A long rotational correlation time of 36 ns was observed for the excited states of the ACs bound to the HSA site responsible for the high ee, suggesting that the ACs have restricted rotational mobility in this site. The ACs in this site have the same prochiral face protected by the protein, and this protection is responsible for the high ee observed. These insights provide a strategy for the rational design of supramolecular photochirogenic systems.",

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AU - Fuentealba, Denis

AU - Kato, Hanako

AU - Nishijima, Masaki

AU - Fukuhara, Gaku

AU - Mori, Tadashi

AU - Inoue, Yoshihisa

AU - Bohne, Cornelia

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AB - The mechanism for the high enantiomeric excess (ee) (80-90%) observed in the photocyclodimerization of 2-anthracenecarboxylate (AC) in the chiral binding sites of human serum albumin (HSA) was studied using fluorescence anisotropy. A long rotational correlation time of 36 ns was observed for the excited states of the ACs bound to the HSA site responsible for the high ee, suggesting that the ACs have restricted rotational mobility in this site. The ACs in this site have the same prochiral face protected by the protein, and this protection is responsible for the high ee observed. These insights provide a strategy for the rational design of supramolecular photochirogenic systems.

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Explaining the highly enantiomeric photocyclodimerization of 2-anthracenecarboxylate bound to human serum albumin using time-resolved anisotropy studies

Abstract

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