Abstract
A selenium nanoparticle binding peptide was isolated from a phage display library and genetically fused to a metalloid reductase that reduces selenite (SeO32-) to a Se0 nanoparticle (SeNP) form. The fusion of the Se binding peptide to the metalloid reductase regulates the size of the resulting SeNP to ∼35 nm average diameter, where without the peptide, SeNPs grow to micron sized polydisperse precipitates. The SeNP product remains associated with the enzyme/peptide fusion. The Se binding peptide fusion to the enzyme increases the enzyme's SeO32- reductase activity. Size control of particles was diminished if the Se binding peptide was only added exogenously to the reaction mixture. The enzyme-peptide construct shows preference for binding smaller SeNPs. The peptide-SeNP interaction is attributed to His based ligation that results in a peptide conformational change on the basis of Raman spectroscopy.