A conformational study of corneal dermatan sulfate proteoglycan using fluorescence spectroscopy

DSPG is a major proteoglycan of the corneal stroma and is thought to be important for the transparency of the tissue. We have studied its conformation by exploring the microenvironment and dynamics of its lone Tryptophan (Trp) residue using steady state and time resolved fluorescence spectroscopy. DSPG exhibits a doublet Trp fluorescence emission. Such a doublet emission has been observed earlier in the copper protein azurin and in avian lens delta-crystallin. Unlike the above cases where the doublet emission is thought to arise due to vibronic structure or the location of Trp at the interface of interacting subunits, fluorescence quenching, denaturation studies and ANS binding with DSPG indicate the location of Trp at two different environments. Such a situation could arise from the differential glycosylation of the core protein or due to duplexation and aggregation of the glycosaminoglycan chains.