Spectroscopic investigation of the interaction of bovine serum albumin with a novel cardiac agent V-09
2008 ◽
Vol 22
(1)
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pp. 43-50
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Keyword(s):
This study employs fluorescence spectroscopy to characterize the binding properties of a newly synthesized cardiac agent, V-09, on bovine serum albumin (BSA). This compound shows the highest cardiac activity in the whole series. The binding constantsKat 25°C and 37°C are obtained, the values are 7.12×104l mol–1, 4.66×104l mol–1, respectively. The standard enthalpy change (ΔH0) and the standard entropy change (ΔS0) are calculated to be –27.13 KJ mol–1and 1.854 J mol–1K–1, which indicated that hydrophobic forces play major role in the interaction between V-09 and BSA. The binding average distance between V-09 and BSA (2.57 nm) is obtained on the basis of the theory of Főrster energy transfer.
2019 ◽
Vol 44
(3-4)
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pp. 198-205
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Keyword(s):
2008 ◽
Vol 31
(14)
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pp. 2077-2088
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2007 ◽
Vol 11
(07)
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pp. 475-480
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