Fractions of thermodynamic functions for native lysozyme adsorption onto moderately hydrophobic surface

Studies on the conformational change of adsorbed BSA onto a moderately hydrophobic surface at different denaturant concentrations and surface coverages

“…The native BSA lost some ordered structure during the adsorption and the adsorption is an exothermic and an 0021-9797/$ -see front matter Ó 2010 Elsevier Inc. All rights reserved. doi:10.1016/j.jcis.2010.01.003 entropy-driven process, which is quite similar to that of lysozyme previously studied in our laboratory [26]. Up to now, it has been an indisputable fact that native protein will undergo conformational loss when adsorbed onto liquid/solid interfaces, but how the conformation of denatured protein changes on adsorption was seldom investigated.…”

Inactivation and Adsorption of Human Carbonic Anhydrase II by Nanoparticles

“…This is also supported by the positive entropic term obtained from the ITC data. In fact, the entropic factors have been highlighted as the main driving force in a number of cases regarding nanoparticle–protein interactions. , This entropic gain can be attributed to conformational changes in the protein that allow more structural freedom as well as release of counterions and hydration water from the contact area between nanoparticles and protein. ,, Therefore, the hydrophobic effect still has an important role as driving force for the interaction between HCAII and PSCOOH.…”

“…37,38 This entropic gain can be attributed to conformational changes in the protein that allow more structural freedom as well as release of counterions and hydration water from the contact area between nanoparticles and protein. 37,39,40 Therefore, the hydrophobic effect still has an important role as driving force for the interaction between HCAII and PSCOOH.…”

Adsorption of folic acid, riboflavin, and ascorbic acid from aqueous samples by Fe3O4magnetic nanoparticles using ionic liquid as modifier

“…Therefore, dehydration entropy, DS d , predominates over adsorption affinity entropy, DS a , and consequently the entropy of adsorption is positive. 39 Since the free energy for hydrophobic interactions is lower than 20 kJ mol À1 (Table 1), the hydrophobic interaction for the adsorption process in the studied temperature range is expected. The change in free energy for physisorption is between 20 and 0.0 kJ mol À1 , but for chemisorption is in the range of 80 to 400 kJ mol À1 .…”