Enhanced fluorescence of proteins and label-free bioassays using aluminum nanostructures.
We report the enhanced intrinsic fluorescence from several proteins in proximity to aluminum nanostructured surfaces. Intrinsic fluorescence in proteins is dominated by the tryptophan residues. Intensities and lifetimes of several proteins with different numbers of tryptophan residues assembled on the surfaces of quartz or aluminum nanostructured films were measured. Immobilized protein molecules on the surface of an aluminum nanostructured film resulted in a significant fluorescence intensity enhancement (up to 14-fold) and lifetime decrease (up to 6-fold) compared to the quartz substrates. These large spectroscopic changes allow design of label-free bioassays where detection of binding interactions between proteins can be observed in the presence of a bulk sample solution. Binding of streptavidin to the biotinylated aluminum surface was demonstrated in the presence of 100 microg/mL bovine serum albumin in the sample solution by measurements of tryptophan intensity and lifetime changes.
Ray
Krishanu
K
Center for Fluorescence Spectroscopy, Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 725 West Lombard St, Baltimore, Maryland 21201, USA.
Szmacinski
Henryk
H
Lakowicz
Joseph R
JR
D000535:Aluminum / Q000737:chemistry*; D000818:Animals; D001681:Biological Assay; D019921:Biotinylation; D002417:Cattle; D005453:Fluorescence; D053768:Metal Nanoparticles / Q000737:chemistry*; D049329:Nanostructures; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012710:Serum Albumin, Bovine / Q000737:chemistry; D014364:Tryptophan / Q000737:chemistry*
D011506:Proteins; D012710:Serum Albumin, Bovine; D014364:Tryptophan; D000535:Aluminum