Conformation, stability and interactions of corneal keratan sulfate proteoglycan.

We have monitored the molecular conformation, stability, interaction and dynamics of keratan sulfate proteoglycan, the major structural protein component of the cornea, in solution, by studying the fluorescence spectral features of its tryptophan residues as component-specific intrinsic spectral probes (collagen, the other structural component of the cornea, has no tryptophans). Our study suggests that the Trp region of the molecule is in a motionally restricted environment as it exhibits a fluorescence red-edge effect and shows dipole relaxation. The extrinsic spectral probe 8-anilinonaphthalene 1-sulfonate reveals keratan sulfate proteoglycan to possess significant surface hydrophobicity. This dual character of keratan sulfate proteoglycan allows us to label it as an 'ambidextran' proteoglycan. The molecule is stable between pH 5-8 and has a Tm value of 72 degrees C. Disulfide bonds play a role in the stability of the molecule. KSPG is seen to interact with collagen and the model compound, poly(L-proline). Interaction of the proteoglycan with unilamellar vesicles appears to be more interfacial than penetrative. This dual interaction displayed by KSPG with collagen and with lipid assemblages suggests that it plays the role of a 'filler' in the extracellular matrix of the cornea.