Plasma protein and antisera interactions with L-cysteine and 3-mercaptopropionic acid monolayers on gold surfaces

Tengvall, Pentti; Lestelius, Magnus; Liedberg, Bo; Lundström, Ingemar

doi:10.1021/la00041a001

Cited by 68 publications

(47 citation statements)

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“…Several of the plasma proteins may interact with gold by chemisorption via disulfide and thiol groups, and it is likely that such chemisorbed proteins would not be elutable by SDS. Effects of this type were noted by Tengvall et al 35 All of the peptide surfaces appear to adsorb more proteins than the unmodified gold; and assuming that proteins adsorbed to bare gold patches that may be present are not eluted by SDS, the proteins seen must be associated with the peptide or cysteine sites. The patterns observed are similar for the various surfaces with all surfaces showing an affinity for albumin, complement proteins, and vitronectin.…”

Section: Discussionmentioning

confidence: 86%

Peptide modified gold-coated polyurethanes as thrombin scavenging surfaces

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Tengvall

et al. 2000

J. Biomed. Mater. Res.

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Thin layers of gold were deposited on polyurethane film and chemisorbed with three peptides having an N-terminal cysteine: Cys-Pro-Arg, Cys-(L)Phe-Pro-Arg, and Cys-(D)Phe-Pro-Arg. The ability of these surfaces to act as thrombin scavengers was evaluated. The peptides are related to the known thrombin inhibitor Phe-Pro-Arg chloromethyl ketone and were shown to have significant thrombin inhibitory activity in solution. Attachment of the peptides to gold was confirmed by water contact angle and X-ray photoelectron spectroscopy measurements. Thrombin adsorption from a buffer and plasma was investigated, and chromogenic substrate assays were carried out for thrombin activity on the surfaces and in the supernatant following adsorption. The data suggest that the peptide-modified surfaces are able to adsorb thrombin with high affinity from a buffer and that thrombin is taken up selectively from plasma. The Cys-(D)Phe-Pro-Arg modified surfaces showed particularly high affinity for thrombin. It was also found that the activity of thrombin adsorbed on the peptide surfaces was inhibited, and inhibition was greatest on the Cys-(D)Phe-Pro-Arg surface. We concluded that the peptide surfaces may have potential as antithrombogenic materials via their ability to scavenge and inhibit thrombin generated as a result of blood-material contact.

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Section: Discussionmentioning

confidence: 86%

Peptide modified gold-coated polyurethanes as thrombin scavenging surfaces

Sun

Sheardown

Tengvall

et al. 2000

J. Biomed. Mater. Res.

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“…The gap size was set as the sum of the SAM thickness for cysteamine and citrate molecules. 31,32 The two particles were moved along the rod tip perimeter to the rod side with 22.5° steps and the spectra were obtained in each position. Due to the asymmetry of the system, different light propagation and polarization directions were simulated and averaged to match closer the ensemble bulk measurement.…”

Section: Please Do Not Adjust Marginsmentioning

confidence: 99%

Assembling patchy nanorods with spheres: limitations imposed by colloidal interactions

et al. 2016

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For gold nanorods the intrinsic shape-anisotropy offers the prospect of anisotropic assembly, provided their regionselective surface modification can be realized. Here we developed a nanorod with patchy surface chemistry, featuring positively charged molecules in the tip region and polymer molecules at the sides by careful control of molecule concentrations during ligand exchange. When these patchy nanorods are assembled with small negatively spherical particles, electric double layer interaction can direct the assembly of two nanospheres at the opposite ends of the nanorods. The PEG chains promote the selectivity of the procedure. As the size of the nanospheres increases, they start to shift towards the side of the nanorod due to increased van der Waals interaction. When the relative size of the nanospheres is even larger, only a single nanoshpere is assembled, but instead of the tip region, they are attached to side of the nanorods. The apparent cross-over of the region-selectivity can be interpreted in terms of colloidal interactions, i.e. the second spherical particle is excluded due to nanosphere-nanosphere electric double layer repulsion, while the large vdW attraction result in a side positioning of the single adsorbed spherical particle. The results underline the importance of absolute values of the different interaction strengths and length scales in the programmed assembly of pathy nanoscale building blocks.

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“…For instance, proteins can be readily immobilized on L-Cys-coated surfaces, yielding very convenient substrates for nanofabrication and patterning involving biological materials. 2 A better understanding of the molecular properties of L-Cys monolayers would certainly help in recognizing the parameters that govern the protein adhesion. The characterization of the monolayer in an electrochemical environment would also be advantageous because proper control over the electrical potential of the interface should allow better regulation of the protein adsorption.…”

Section: Introductionmentioning

confidence: 99%

Investigation of the Adsorption of l-Cysteine on a Polycrystalline Silver Electrode by Surface-Enhanced Raman Scattering (SERS) and Surface-Enhanced Second Harmonic Generation (SESHG)

2002

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The adsorption of L-cysteine (L-Cys) onto a polycrystalline silver electrode surface was investigated by in situ spectroelectrochemical methods. Surface-enhanced Raman spectroscopy (SERS) and surface-enhanced second-harmonic generation (SESHG) measurements were performed in a 0.2 M KCl solution in the presence and absence of L-Cys. The experimental results indicated that L-Cys strongly adsorbs onto silver and remains on the surface at potentials as negative as -900 mV (vs Ag/AgCl). A peak around -650 mV was observed in the SESHG intensity versus applied potential plots obtained in the presence of L-Cys. The peak was indicative of an abrupt change in the electronic properties of the interface at that potential. The SERS spectra at potentials more negative than ca. -650 mV showed an increase in the intensity of vibrational modes assigned to the carboxylate group of L-Cys. The combination of the SERS and the SESHG results suggests a potentialinduced reorientation of the adsorbed L-Cys molecules for potentials more negative than -650 mV. The data interpretation considered the different possible conformational forms of L-Cys adsorbed on the Ag surface. At potentials more positive than ca. -650 mV, L-Cys molecules adsorb with the protonated amino group pointing toward the surface. In this case, the positively charged amino group is stabilized by the coadsorbed chloride anions. The molecule changes its conformation at potentials more negative than -650 mV as the chloride ions leave the surface. The C R -C bond rotation brings the carboxylate group closer to the surface at these potentials.

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Plasma protein and antisera interactions with L-cysteine and 3-mercaptopropionic acid monolayers on gold surfaces

Cited by 68 publications

References 0 publications

Peptide modified gold-coated polyurethanes as thrombin scavenging surfaces

Peptide modified gold-coated polyurethanes as thrombin scavenging surfaces

Assembling patchy nanorods with spheres: limitations imposed by colloidal interactions

Investigation of the Adsorption of l-Cysteine on a Polycrystalline Silver Electrode by Surface-Enhanced Raman Scattering (SERS) and Surface-Enhanced Second Harmonic Generation (SESHG)

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