Hydrodynamic properties of human adhesion/growth-regulatory galectins studied by fluorescence correlation spectroscopy.

摘要: Fluorescence correlation spectroscopy is applied on homologous human lectins (i.e., adhesion/growth-regulatory galectins) to detect influence of ligand binding and presence the linker peptide in tandem-repeat-type proteins hydrodynamic properties. Among five tested proteins, lactose increased diffusion constant only cases homodimeric galectin-1 linkerless variant galectin-4. To our knowledge, close structural similarity among galectins does not translate into identical response binding. Kinetic measurements show association dissociation rate constants order 1 103 M−1 s−1 10−4 s−1, respectively. Presence protein leads anomalous scaling with molecular mass. These results provide what we believe be new insights lectin responses glycan binding, detectable so far by small angle neutron scattering, relevance peptide. Methodologically, fluorescence shown a rather simple technical tool characterize properties these at high level sensitivity.