Blood glycoprotein from antarctic fish. Possible conformational origin of antifreeze activity

High resolution 1H NMR and circular dichroism (CD) measurements have been performed on aqueous solutions of antarctic fish antifreeze glycoprotein. The carbohydrate contribution ot the observed CD spectrum has been estimated from closely analogous model compounds. The residual peptide contribution cannot be interpreted of the known spectral behaviour of alpha-helix, beta-sheet and random coil. Instead it resembles the CD spectrum of beta-structure in position, magnitude and spectral form, but is of opposite sign, indicating a specific but unusual peptide conformation, which we suggest may be stabilised by non-bonded interactions between the peptide backbone and the carbohydrate sidechains. Previous evidence which supports this interpretation is reviewed. NMR and CD measurements between -2 and +30 degrees C are consistent with conformational stability throughout the biologically relevant temperature range. The mechanism of the antifreeze activity is discussed in terms of the spatial and orientational correlations of sugar hydroxy groups and water in the liquid and solid states. The implication of an ordered peptide structure is explained by the comparison of the antifreeze glycoprotein with synthetic water-soluble polymers which also exhibit limited antifreeze properties.