Characterization of Ferritin Adsorption onto Gold

Caruso, Frank; Furlong, D. Neil; Kingshott, Peter

doi:10.1006/jcis.1996.4625

Cited by 174 publications

(163 citation statements)

References 22 publications

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“…Morphology of Protein Homo-oligomers-AFM images of mammalian drug-metabolizing P450s dried on mica (46) and in lipid nanodiscs (47) (and references therein) have been reported, as have peptides and other proteins (27)(28)(29)(30)(31). Our high resolution images of steroidogenic P450c17 and P450arom (Fig.…”

Section: Protein-lipid and Protein-protein Interactions Studied By Qcsupporting

confidence: 55%

Organization of Cytochrome P450 Enzymes Involved in Sex Steroid Synthesis

Praporski

Nguyen

et al. 2009

Journal of Biological Chemistry

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Mounting evidence underscores the importance of proteinprotein interactions in the functional regulation of drug-metabolizing P450s, but few studies have been conducted in membrane environments, and none have examined P450s catalyzing sex steroid synthesis. Here we report specific protein-protein interactions for full-length, human, wild type steroidogenic cytochrome P450 (P450, CYP) enzymes: 17␣-hydroxylase/ 17,20-lyase (P450c17, CYP17) and aromatase (P450arom, CYP19), as well as their electron donor NADPH-cytochrome P450 oxidoreductase (CPR). Fluorescence resonance energy transfer (FRET) 3 in live cells, coupled with quartz crystal microbalance (QCM), and atomic force microscopy (AFM) studies on phosphatidyl choline ؎ cholesterol (mammalian) biomimetic membranes were used to investigate steroidogenic P450 interactions. The FRET results in living cells demonstrated that both P450c17 and P450arom homodimerize but do not heterodimerize, although they each heterodimerize with CPR. The lack of heteroassociation between P450c17 and P450arom was confirmed by QCM, wherein neither enzyme bound a membrane saturated with the other. In contrast, the CPR bound readily to either P450c17-or P450arom-saturated surfaces. Interestingly, N-terminally modified P450arom was stably incorporated and gave similar results to the wild type, although saturation was achieved with much less protein, suggesting that the putative transmembrane domain is not required for membrane association but for orientation. In fact, all of the proteins were remarkably stable in the membrane, such that high resolution AFM images were obtained, further supporting the formation of P450c17, P450arom, and CPR homodimers and oligomers in lipid bilayers. This unique combination of in vivo and in vitro studies has provided strong evidence for homodimerization and perhaps some higher order interactions for both P450c17 and P450arom.

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Section: Protein-lipid and Protein-protein Interactions Studied By Qcsupporting

confidence: 55%

Organization of Cytochrome P450 Enzymes Involved in Sex Steroid Synthesis

Praporski

Nguyen

et al. 2009

Journal of Biological Chemistry

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“…Saturation adsorption of HSA and FER is approximately of 2.5 × 10 −7 and 6.3 × 10 −7 g/cm 2 , respectively [18,37]. Corresponding thicknesses of the adsorbed HSA or FER layers are expected to approach each protein's molecular dimensions.…”

Section: Discussionmentioning

confidence: 99%

Albumin binding and insertion into PS-b-PEO monolayers at air–water interface

Hlady

Jogikalmath

2007

Colloids and Surfaces B: Biointerfaces

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Interaction of human serum albumin with poly(styrene)-b-poly(ethylene oxide) (PS-b-PEO) monolayer at air/solution interface was studied by measuring surface pressure. The density of PEO chains in the monolayer was controlled using Langmuir trough barriers. The thickness of PS-b-PEO monolayer prior to and after albumin adsorption was computed from in situ surface plasmon resonance (SPR) measurements. Depending on the initial PEO surface density the surface pressure kinetics of albumin insertion displayed two different regimes: below the PEO "pancake-brush" transition albumin binding was initially very rapid and itself induced the "pancake-brush" transition in the monolayer, and above the "pancake-brush" transition where some albumin penetration into the free PS-b-PEO monolayer still occurred into the PEO "brush". In the case of SPR-immobilized monolayer, more than 0.1 PEO chain/nm 2 was required to inhibit albumin or ferritin adsorption. A half-reduction of albumin adsorption required approx. threefold higher PEO surface density than the half-reduction of ferritin adsorption.

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“…For thin, evenly distributed, and rigid films, an adsorption-induced ⌬f is related to mass uptake (⌬m) via the Sauerbrey relation (31): ⌬f ϭ Ϫn⌬mC Ϫ1 , where C (equivalent to 17.7 ng cm Ϫ2 Hz Ϫ1 ) is the mass sensitivity constant and n is the overtone number. However, for proteins adsorbed from the aqueous phase, one must also be aware that water hydrodynamically coupled to the adlayer is included in the measured mass uptake (32). In addition, when the adsorbed material is nonrigid, additional energy dissipation (viscous loss) is also induced.…”

Section: Qcm-d Analysismentioning

confidence: 99%

C3 Adsorbed to a Polymer Surface Can Form an Initiating Alternative Pathway Convertase

Andersson

Ekdahl

Larsson

et al. 2002

The Journal of Immunology

134

109

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Contact between blood and a biomaterial surface induces an immediate complement-mediated inflammatory response. Under these conditions, the alternative pathway of complement is often initiated and amplified on the biomaterial surface. Adsorption of a protein such as C3 to a polymer surface induces conformational changes in the protein. Based on the expression on adsorbed C3 of conformational neoepitopes specific for bound C3 fragments, we have hypothesized that adsorbed C3 is able to bind factor B and form a functional C3,Bb convertase. Using a quartz crystal microbalance to monitor binding of proteins to a polymer surface, we have demonstrated that a functional C3-containing alternative pathway convertase can be formed, in particular, in the presence of properdin. These data indicate that adsorption of C3 induces conformational changes that turn C3 into a C3b-like molecule that is able to participate in the functioning of the alternative convertase, and they suggest a new mechanism for complement activation on a biomaterial surface.

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Characterization of Ferritin Adsorption onto Gold

Cited by 174 publications

References 22 publications

Organization of Cytochrome P450 Enzymes Involved in Sex Steroid Synthesis

Organization of Cytochrome P450 Enzymes Involved in Sex Steroid Synthesis

Albumin binding and insertion into PS-b-PEO monolayers at air–water interface

C3 Adsorbed to a Polymer Surface Can Form an Initiating Alternative Pathway Convertase

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