One- and Two-Photon Brightness of Proteins Interacting with Gold. A Closer Look at Gold-Insulin Conjugates
Abstract
Red luminophores displaying large Stokes shift and high-quantum yields are obtained when gold salts are reacted with proteins under strongly alkaline conditions. Although bovine serum albumin (BSA) has mainly been used as a protein template, other attempts to prepare red luminophores have been proposed using other proteins. Here, we report on the structural characterization and nonlinear optical properties of insulin-gold conjugates. Such conjugates display strong luminescence at ≈670 nm with quantum yields that reach 5.4%. They also display long luminescence lifetimes allowing efficient reactive oxygen species generation, with a quantum yield of 1O2 generation reaching ~10%. In addition, they exhibit remarkable nonlinear optical properties and in particular a strong two-photon excited fluorescence (TPEF) cross section in the range of 800-1100 nm. By combining experimental studies and time‐dependent density functional theory simulations (TD‐DFT), we show the formation of Insulin-Au(III) conjugates.The interaction of Au(III) ions with the aromatic rings of tyrosine induces charge transfer-like excitations in the visible range. Experimental investigations, together with molecular dynamics simulations of insulin and calculations of electronic properties in a model system, are performed to explore the origin of optical features and the structure-optical property relationship, leading the way to new concepts for nonlinear optics using protein-Au(III) conjugates.
- This article is part of the themed collection: Metal nanoclusters