Binding of harmane to human and bovine serum albumin: fluorescence and phosphorescence study

• Autorzy: Gałęcki K , Despotović B , Ioannidis A.-G , Janani T , Galloway C , Nakamura Y , Oluyinka G
• Języki publikacji: EN

Abstrakty

EN

The binding of harmane with human serum albumin (HSA) and bovine serum albumin (BSA) were studied by fluorescence and phosphorescence spectroscopic methods. Quenching of fluorescence of serum albumins by harmane was found to be a static quenching process. The equilibrium constant (K) of complex formation was found to be equal to (5.16±0.28)x10⁴ M^-1 and (4.32±0.30)x10⁴ M^-1 for HSA and BSA, respectively. It was found that the interactions of harmane with HSA and BSA were also in the excited triplet state. The determined bimolecular constant or triplet state quenching (k_q^T)of the proteins studied by harmane was (1.15± 0.10)x10⁷ M^-1 s^-1 and (2.88±0.22)x10⁷ M^-1 s^-1 for HSA and BSA, respectively. Based on the similar value of K and k_q^T for HSA and BSA, a possible suggestion is that, most probably, the binding site of harmane is located in the drug site 1 in the subdomain IIa.

Słowa kluczowe

EN

human serum albumin; bovine serum albumin; harmane; fluorescence; phosphorescence

PL

albumina surowicza ludzka; albumina surowicza wołowa; fluorescencja; fosforescencja

• Wydawca: Wydawnictwo Politechniki Łódzkiej
• Czasopismo: Biotechnology and Food Science
• Rocznik: 2012
• Tom: Vol. 76, nr 1
• Strony: 3--12
• Opis fizyczny: Bibliogr. 25 poz., wykr.

Twórcy

autor

Gałęcki K

• Institute of General Food Chemistry, Lodz University of Technology, 90-924 Lodz, Poland

autor

Despotović B

• University of Sarajevo, 71000, Sarajevo, Bosnia and Hercegowina

autor

Ioannidis A.-G

• Agricultural University of Athens, 11855, Athens, Greece

autor

Janani T

• Norwegian University of Science and Technology, 7491, Trondheim, Norway

autor

Galloway C

• University of Newcastle Upon Tyne, NE1 7RU, Newcastle Upon Tyne, England

autor

Nakamura Y

• Kyushu University, 8120053, Fukuoka, Japan

autor

Oluyinka G

• University of Greenwich, SE10 9LS, London, England

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