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Throughout 4.5 billion year of molecular evolution, proteins have evolved in order to maintain the spatial proximity between aromatic residues (Trp, Tyr and Phe) and disulphide bridges (SS) (Petersen et al, 1999). Aromatic residues are the nanosized antennas in the protein world that can capture UV light (from ~250-298nm). Once excited by UV light they can enter photochemical pathways likely to have harmful effects on protein structures. However, disulphide bridges in proteins are excellent quenchers of the excited state of aromatic residues, contributing this way to protein stability and activity. UV light excitation of the aromatic residues is known to trigger electron ejection from their side chains (Bent & Hayon, 1975a; Bent & Hayon, 1975b; Bent & Hayon, 1975c; Creed, 1984a; Creed, 1984b; Kerwin & Rammele, 2007, Neves-Petersen et al., 2009a). These electrons can be captured by disulphide bridges, leading to the formation of a transient disulphide electron adduct radical, which will dissociate leading to the formation of free thiol groups in the protein. This observation lead to the development in our lab of a new photonic technology, Light Assisted Molecular Immobilization (LAMI), used to functionalize surfaces with biomolecules. This technology is being used in order to create a new generation of biosensors with unsurpassed density (number of spots per mm2). This technology is also being used in order to create nanoparticles based drug delivery systems relevant to nanomedical applications (Parracino et al., 2011).

UV Light Effects on Proteins: From Photochemistry to Nanomedicine