Surface charge, human serum albumin

The cooperative effect of charges and hydrophobic functions on protein complexation was also investigated in another study using poly 9,9-bis[6 -(ArfiST,N-trimethylammonium)he g l](fluorophenylene) bromide /human serum albumin nanoparticles. In this case, the formation of assemblies with high affinity was the result of a combination of electrostatic interactions between the cationic side chains of the polymer and the negatively charged surface of the protein, in addition to the hydrophobic interactions between the polymer backbone and the hydrophobic patches of the protein. 

TABLE 4 Summary of the Isoelectric Points and the Charge Densities " of Investigated Snrfaces and the Observed Adsorbed Areal Density of PLL 75)-g[5.6]-PEG(5), Serum, and Human Serum Albumin (HSA) on Unmodified Surfaces and of Serum and HSA on PLL(375)-g[5.6]-PEG(5>Modified Surfaces"... 

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