Nanochemistry offers stimulating opportunities for a wide variety of applications in the biosciences. Understanding of
the interaction of nanoparticles with biomolecules such as proteins is very important as it can help better design and
fabricate nanocomposites for applications in diagnostics, drug delivery, and cell monitoring. In this work, the interaction
of Bovine Serum Albumin (BSA) and two types of metal oxide nanoparticles (titanium and tin) have been studied using
the intrinsic fluorescence of tryptophan residue from the proteins measured by steady state and time resolved
fluorescence techniques. The nanoparticles which were fabricated using a novel synthetic process have average sizes of
~2 nm (SnO2) and ~6 nm (estimated for TiO2) and have very high solubilities in a variety of solvents. The Stern-Volmer
plots indicate an effective quenching process by TiO2 nanoparticles whereas SnO2 nanoparticles have a lower quenching efficiency for BSA fluorescence. Static quenching is the major contribution in the overall process which may indicate a
high degree of association between protein and nanoparticles. The difference in BSA fluorescence quenching efficiency
between the two types of nanoparticles can be explained by the non-covalent interaction differences and the thermal
stability of protein-nanoparticle associated species for both materials.
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