The effects of heavy water on 8-Anilino-1-naphthalenesulfonic acid binding to bovine serum albumin
The binding of 8-Anilino-1-naphthalenesulfonic acid (ANS) to bovine serum albumin (BSA) is mediated by hydrophobic interactions. This interaction results from the entropically unfavorable structuring of water near hydrophobic surfaces. How this effect changes as regular light water (H2O) is substituted for heavy water (D2O) is largely unexplored. To investigate this question, we are examining the binding behavior of ANS with BSA in heavy and light water as measured by fluorescent spectroscopy. To date, we have observed that ANS quantum yield is increased in the presence of D2O versus H2O. Understanding this alteration in ANS binding in these solvents will improve our understanding regarding hydrophobicity and may have implications for improving protein stability.
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