2014
DOI: 10.1039/c4cp00293h
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Human serum albumin binding to silica nanoparticles – effect of protein fatty acid ligand

Abstract: Neutron reflectivity shows that fatted (F-HSA) and defatted (DF-HSA) versions of human serum albumin behave differently in their interaction with silica nanoparticles premixed in buffer solutions although these proteins have close to the same surface excess when the silica is absent. In both cases a silica containing film is quickly established at the air-water interface. This film is stable for F-HSA at all relative protein-silica concentrations measured. This behaviour has been verified for two small silica … Show more

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Cited by 17 publications
(16 citation statements)
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“…In addition, since the HSA protein can hardly adsorb on negatively charged nanoparticles (with no hydrophobic part) due to the repulsively electrostatic interaction 44 , it is not necessary to coat stealth polymers onto their surface for HSA protein resistance. But notice that the surface of negatively charged nanoparticles in real experiments may be semi-hydrophilic or partially hydrophobic, thus the HSA protein could adsorb onto their surface 48 . However, the main driving force for protein adsorption in those cases is hydrophobic interaction (instead of electrostatic interaction) 48 , which is similar to that in the case of hydrophobic nanoparticles.…”
Section: Resultsmentioning
confidence: 99%
“…In addition, since the HSA protein can hardly adsorb on negatively charged nanoparticles (with no hydrophobic part) due to the repulsively electrostatic interaction 44 , it is not necessary to coat stealth polymers onto their surface for HSA protein resistance. But notice that the surface of negatively charged nanoparticles in real experiments may be semi-hydrophilic or partially hydrophobic, thus the HSA protein could adsorb onto their surface 48 . However, the main driving force for protein adsorption in those cases is hydrophobic interaction (instead of electrostatic interaction) 48 , which is similar to that in the case of hydrophobic nanoparticles.…”
Section: Resultsmentioning
confidence: 99%
“…The same is also true of NP assembly into chains, sheets, twisted ribbons, and shells (6,7,36,61,62), as well as for assemblies of NPs with other chemical species. When NPs are combined with proteins, multiple examples of discontinuities and counterintuitive trends are ascribed to "patchy" interactions (63)(64)(65)(66). Many parallels in the behavior of NPs and globular proteins should also be noted (15,67,68).…”
Section: Illustration Of Deviationsmentioning
confidence: 95%
“…18 Indeed it was argued in one fairly early study, 19 and is now becoming increasingly common, for layer roughness values whose minimum are consistent with the presence of capillary waves to be applied in models used to fit neutron reflectivity data at fluid interfaces. 20,21 Higher layer roughness values have been used in studies on proteins and nanoparticles 22 or crosslinked polymer nanogels 23 at the air/water interface. Also, in one early study on monolayers of hexadecyltrimethylammonium bromide that exploited kinematic data analysis, it was commented that the air/water interface is even rougher than that predicted from a simple capillary wave model.…”
Section: Introductionmentioning
confidence: 99%