The characterization of keratin-chicken egg white-templated luminescent Au cluster composite films
were studied using fourier-transform infrared spectroscopy (FTIR) to demonstrate and quantify the
secondary transformation of composite films. The results showed that the secondary structure of treated
films was transformed from disordered structure to ordered conformation including a-helix conformation
and b-pleated-sheet conformation due to the increase of protein-templated luminescent Au cluster.
The absorption features of treated films were exhibited by the UVevis spectra. The bule-shift and
decreased intensity indicated the change of microenvironment due to the concentration of proteintemplated
luminescent Au cluster. The transmission electron microscopy images of composite films
supported the aggregation resulting from microenvironment. The effect of protein-templated luminescent
Au cluster was characterized by the laser scanning confocal microscope (LSCM) images which
showed the gradually intensive luminescence with increasing Au cluster and the transformation from the
whiskers to nanoparticle.