Interaction of 4-Nitroaniline with Serum Albumin

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Abstract:

Bovine serum albumin (BSA) and human serum albumin (HSA) interaction with 4-nitroaniline was investigated by fluorescence spectroscopy respectively. 4-Nitroaniline can strongly quench intrinsic fluorescence of BSA and HSA. 4-Nitroaniline exhibits a high affinity to bovine and human serum albumins. The binding constants K and the number binding site n were obtained by double-log regression equation. Negative enthalpy (ΔH) and positive entropy (ΔS) values indicated that both hydrogen bond and hydrophobic forces played a major role in the binding of 4-nitroaniline and SA. The results of synchronous fluorescence showed the polarity around tryptophan residues was decreased and the hydrophobicity was increased.

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337-340

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February 2014

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© 2014 Trans Tech Publications Ltd. All Rights Reserved

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