Teeth and bones: applications of surface science to dental materials and related biomaterials

Protein binding on metallic implant surfaces, such as titanium, is governed by the physico-chemical nature of the metallic surface. Human plasma fibronectin (HPF) is an important matrix glycoprotein that mediates cell and protein attachment to each other or to the extracellular matrix present during wound healing. The objective of this study was to investigate the adsorption of HPF onto polished commercially pure titanium (cpTi) by using atomic force microscopy (AFM) and electron spectroscopy for chemical analysis (ESCA) and to measure the resultant surface contact angle before and after HPF binding. Two types of cpTi disks, one highly polished in our laboratory (HSS) and one commercially prepared (31), were reacted with HPF solutions of varying concentrations (1 microg/mL-10 ng/mL). ESCA survey spectra of samples coated with 1 microg/mL of fibronectin showed an increase in organic nitrogen and carbon compared with uncoated controls. Contact angle measurements of HSS and 31 cpTi disks showed no significant difference in average contact angle (36.3 degrees +/- 3.5 and 39.1 degrees +/- 3.1) despite differences in local root mean square (RMS) surface roughness (4.45 +/- 0.46 nm and 22.37 +/- 4.17 nm) as measured by AFM. Images obtained by AFM showed that 31 specimens were more irregular, with large parallel polishing grooves. Adsorbed HPF appeared in a globular form with an average length of 16.5 +/- 1.0 nm, a height of 2.5 +/- 0.5 nm, and a width of 9.6 +/- 1.2 nm. Fibronectin coating on both HSS and 31 cpTi specimens resulted in a significant increase in hydrophobicity compared to uncoated specimens. These results indicate the significance of HPF on cpTi and may explain how cpTi implants function in situ.

Surface analysis of human plasma fibronectin adsorbed to commercially pure titanium materials

Prostate cancers express MUC1, but nearly all metastatic cells lack HLA class I molecules. Thus, a lymphocyte population that can sense its antigenic environment, while also able to react to stimuli of natural killer (NK) cells, may be a more versatile effector cell population for antitumor immune responses. Herein, we report that tumor-specific MUC1 peptide, interleukin 2, and interleukin 12 act synergistically to stimulate the ex vivo expansion of CD8+CD56− T cells and CD8+CD56+ natural killer T (NKT) cells from the peripheral blood mononuclear cells of prostate cancer patients, as well as healthy male and female donors. Both the CD56+ NKT cells and CD56− T cells lysed allogeneic mucin-bearing target cells, as well as NK target cells, but not lymphokine-activated killer target cells. However, the CD56+ NKT cells displayed a 2-fold greater cytolytic activity than the CD56− T cells. The mucin-specific cytolytic activity and NK cytolytic activities for both lymphocyte populations were independent of HLA class I and CD1 molecules. The CD56− T cells up-regulated CD56 with continued antigenic stimulation in the presence of interleukin 12, suggesting that CD8+CD56− T cells are NKT cells. However, CD56+ NKT cells expand poorly to continued stimulation. All mucin-stimulated NKT cells exhibited the activated/memory CD45RO phenotype. The NKT cell lines express the α/β T-cell receptor (TCR). The TCR repertoire was limited and varied with cell line, but was not the Vα24Vβ11 TCR typically associated with NKT cells. Whereas CD161 is generally considered a marker of NKT cells, the mucin-stimulated NKT cells did not express this marker. Thus, we have described two phenotypically distinct NKT types that do not display a biased TCR repertoire, but do display specificity for a tumor-specific peptide antigen (CTL-like activity), as well as HLA class I-deficient target cells (NK-like activity).

https://cancerres.aacrjournals.org/content/canres/64/3/1171.full.pdf

Ex Vivo Expansion of CD8+CD56+ and CD8+CD56− Natural Killer T Cells Specific for MUC1 Mucin

A comparative investigation of seed storage protein fractions: The synergistic impact of molecular properties and composition on anisotropic structuring

Design and Expression of a Synthetic Mucin Gene Fragment inEscherichia Coli

X-ray photoelectron spectroscopy (XPS) is a surface sensitive analytical technique that measures the binding energy of electrons in atoms and molecules on the surface of a material. XPS was used to determine the distribution of the oligosaccharide side chains in the glycoprotein, MUC1 mucin. Low-resolution XPS spectra provided elemental composition of MUC1 mucin (fully glycosylated), mucin polypeptide (nonglycosylated), and carbohydrates found in mucin. The nitrogen content of MUC1 mucin was determined to be intermediate between the mucin polypeptide and the carbohydrates. Assuming a uniform distribution of carbohydrate on MUC1 mucin, the average thickness of the carbohydrate layer was calculated to be 4.9 nm using the low-resolution N 1s signals. High-resolution XPS spectra give detailed information about the chemical bonding of the surface molecules. Calculations based on the high-resolution O 1s spectra showed a carbohydrate thickness of 6.6 nm. These experimentally determined values agree reasonably well with an estimated 5 nm of carbohydrate thickness from a simple model which assume that the core protein is a rodlike molecule approximately 5 nm in diameter. Although the carbohydrate coating on the MUC1 mucin appears to be thick enough to cover the core protein entirely, fully glycosylated breast milk MUC1 mucin is susceptible to proteolytic digestion without removal of any oligosaccharide side chain, suggesting areas of exposed core protein. A possible explanation is that the oligosaccharide side chains may form patches of carbohydrate along the core protein with regions of exposed core protein.

Surface structure of human mucin using X-ray photoelectron spectroscopy.

X-ray photoelectron spectroscopy (XPS) is a surface sensitive analytical technique which measures the binding energy of electrons in atoms and molecules. The binding energy can be related to the molecular bonding or oxidation state of an element in the outermost layer of a material, that is 100 A. Thus, XPS is able to identify chemical species present on the surface of a molecule. In this paper XPS is briefly described. Spectra demonstrating its potential use for probing the surface properties of amino acids, polypeptides, proteins, carbohydrates and glycoproteins are discussed.

X-Ray Photoelectron Spectroscopy of Amino Acids, Polypeptides and Simple Carbohydrates

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Surface structure of human mucin using X-ray photoelectron spectroscopy.

X-Ray Photoelectron Spectroscopy of Amino Acids, Polypeptides and Simple Carbohydrates