Peptide-modified surfaces

Fig. 12 Illustration outlining MIP film fabrication. The C-terminus nonapeptide epitope is attached through a tether to a glass or oxidized silicon surface by the N-terminal amino acid of the peptide. Monomers are photochemically cross-linked while remaining in contact with the peptide modified surface. Following polymerization, the glass substrate is removed. The protein can now bind to the MIP via its C-terminus nonapeptide epitope. Modified from [114]...

Many materials have been modified to contain covalently immobilized adhesive peptide sequences, as summarized in Table III [reviewed in Harbers et al. (2002) and West and Hubbell (1997)]. Interaction of cells with peptide-modified surfaces can occur directly, without mediation by adsorbed proteins. Issues that affect selectivity in cellular attachment to peptide-modified surfaces include spacer length, peptide surface... 

Peptide-Modified Surface. On the peptide-modified surface, GMH, no significant chemical shifts from MH were observed. The concentration of the newly introduced thiolether group is too low to be detected with confidence. The guanidinyl C Is (289.0 eV) and amide C Is (288.2 eV) overlap the imide and amide C Is. Carboxyl, hydroxyl, and amide 01s peaks at around 532 eV overlap Si—O and carbonyl 0 Is. The guanidinyl (C—NH) N Is at around 402 eV overlaps the protonated amines. However, the significant increase of the relative peak areas of N Is, of 0 Is above 532.0 eV, and of C Is above 288.0 eV, as well as the decrease of the Ti 2p and Si 2p, are consistent with the presence of peptides. 

M.J. Ernsting, G.C. Bonin, M. Yang, R.S. Labow, J.P. Santerre, Generation of cell adhesive substitutes using peptide fluoroalkyl surface modifiers, Biomaterials 26 (2005) 6536-6546. 

Brandley and Schnaar [140] immobilized a synthetic nonapeptide, Tyr- Ala-Val Thr-Gly Arg-Gly-Asp-Ser, on a polyacrylamide gel, which had been prepared by a ternary copolymerization of acrylamide, bisacrylamide and the acrylic ester of. V-hydroxysuccinimide. They reported that Balb/c 3T3 mouse fibroblast cells (in Hepes-buffered Dulbecco s modified Eagle medium) adhered readily to the peptide-derivatized surfaces, even in the absence of serum, although long-term cell growth required the presence of serum. It was noticed that reference nonapeptide. Tyr-Arg-Leu-Glu-Asp-Pro-Ala-Met-Trp, which has no RGD sequence, failed to promote cell-attachment. 

Scheme 13.1 illustrates the steps in the construction of the peptide-modified electrode. Place a clean gold electrode in 10 mM MPA in 75% ethanol and 25% water. Allow self-assembly of MPA onto the gold surface to occur overnight. Rinse electrodes with absolute ethanol. If the redox potential of the metal to be analysed is outside the potential region between —0.4 and 0.5 V it is recommended that thioctic acid be used for greater stability instead of MPA [2],... 

Figure 7 Protein microarrays and their applications. Ligands, such as proteins, peptides, antibodies, antigens, allergens, and small molecules, are immobilized in high density on modified surfaces to form functional and analytical protein microarrays. These protein microarrays can also be used for various kinds of biochemical analysis.

This chapter presented the surface characterization of disulfide-linked Fc-peptide [Fc-Gl(OBz)CSA] 1, [Fc-Gl(OH)CSA] 2, [Fc-G20MeCSA]j 3, and [Fc-G2(OMe) CSA] 4. These systems have a disulfide group that was used for immobilization on An. On gold surfaces, the acids, unlike the corresponding esters, formed multilayers held together by intermolecular H-bonding. Monolayer coverages, however, are attainable by sonication in mixtures of solvents. CV measurements in the presence of [Fe(CN) ] " reveal that the Fc-peptide-modified electrodes exhibit excellent barrier properties. 

Modified surfaces of sample plates can be used for the affinity capture of analytes from crude mixtures directly on target. Such surfaces can significantly enhance detection sensitivity and can be used for simple sample clean-ups. Titania (Ti02)-coated surfaces, particles or sol-gel systems, for example, have been shown to concentrate phosphopeptides very selectively from peptide fingerprint samples [154, 155]. 

Figure 2. Schematic representation of the modification route. Surface Ti water-vapor—plasma-pretreated titanium. Surface A poljr(3-aminopropyl)siloxane pendant surface. Surface M maleimide-modified surfaces with different alkyl chains. Surface P peptide- or L-cysteine-modified surfaces. H-SR L-cysteine, RGDC, and GRGDSPC.

Table 2. XPS Atomic Ratios N/Si for APS-, Maleimide-, and Peptide- (or L-Cysteine-) Modified Surfaces and the Reaction Yields (Rx-f) Estimated Using Formulas 1 and 2 (See Text, Section 3.3)...

Figure 6. The dependence of the atomic ratios N/Si (XPS) of the peptide- or L-cysteine-modified surfaces on the incubation time.

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