Surface analysis of human plasma fibronectin adsorbed to commercially pure titanium materials.
Surface analysis of human plasma fibronectin adsorbed to commercially pure titanium materials.
复制标题
吸附到商业纯钛材料上的人血浆纤连蛋白的表面分析。
DOI:
10.1002/(sici)1097-4636(199807)41:1
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发表时间:
1998
期刊:
影响因子:
--
通讯作者:
Boskey,AL
中科院分区:
文献类型:
--
作者:
MacDonald,DE;Markovic,B;Allen,M;Somasundaran,P;Boskey,AL
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 μg/mL—10 ng/mL). ESCA survey spectra of samples coated with 1 μg/mL of fibronectin showed an increase in organic nitrogen and carbon compared with uncoated controls. Contact angle measurements of HSS and 3I cpTi disks showed no significant difference in average contact angle (36.3° ± 3.5 and 39.1° ± 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 3I 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 3I 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 functionin situ. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res, 41, 120–130, 1998.