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Present work reports on Cytochrome C (Cyt C) adsorption from solution and as sub-micron sized colloidal particles (pH 7.5) at fluid/solid interface. The colloidal particles from 2 methods ((method 1 freeze-thaw); method 2-Decane/water interface) have been characterized by UV-Visible spectroscopy, Static and Time resolved Fluorescence spectra and Circular dichroic spectroscopy. Morphology and size studies indicate that the colloids are solid and well-packed. Using Quartz crystal microbalance with dissipation, elastic compliance of the protein on quartz surface has been monitored. Properties of the protein from solution and as colloids assembled from method 2 are similar in elastic compliance (65.53 ± 1.2 and 73.5 ± 1.1 GPa respectively) due to polar/non-polar interactions at the solid surface. For particles from method 1, irregular desolvation of water on the particle surface results in higher compliance (104.3 ± 1.3 GPa). Change in work of adhesion from contact angle profiles shows optimal adhesion for colloids from method 1 whereas the protein solution and as colloids from method 2, show subnormal adhesion. The work shows the role of extensive H-bonding with the hydrodynamically coupled water leads to a fluid like system in protein colloids from method 1 whereas those from method 2 behaved more like the pure protein adsorbing from solution.
This article was published in the following journal.
Name: International journal of biological macromolecules
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