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不同不锈钢等级表面蛋白相互作用:蛋白吸附、表面变化和金属释放的影响。

Surface-protein interactions on different stainless steel grades: effects of protein adsorption, surface changes and metal release.

机构信息

Division of Surface and Corrosion Science, Department of Chemistry, School of Chemical Science and Engineering, KTH Royal Institute of Technology, Stockholm, Sweden.

出版信息

J Mater Sci Mater Med. 2013 Apr;24(4):1015-33. doi: 10.1007/s10856-013-4859-8. Epub 2013 Feb 2.

DOI:10.1007/s10856-013-4859-8
PMID:23378148
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3620448/
Abstract

Implantation using stainless steels (SS) is an example where an understanding of protein-induced metal release from SS is important when assessing potential toxicological risks. Here, the protein-induced metal release was investigated for austenitic (AISI 304, 310, and 316L), ferritic (AISI 430), and duplex (AISI 2205) grades in a phosphate buffered saline (PBS, pH 7.4) solution containing either bovine serum albumin (BSA) or lysozyme (LSZ). The results show that both BSA and LSZ induce a significant enrichment of chromium in the surface oxide of all stainless steel grades. Both proteins induced an enhanced extent of released iron, chromium, nickel and manganese, very significant in the case of BSA (up to 40-fold increase), whereas both proteins reduced the corrosion resistance of SS, with the reverse situation for iron metal (reduced corrosion rates and reduced metal release in the presence of proteins). A full monolayer coverage is necessary to induce the effects observed.

摘要

使用不锈钢(SS)进行植入是一个例子,在评估潜在的毒理学风险时,了解 SS 从蛋白质诱导的金属释放非常重要。在这里,在含有牛血清白蛋白(BSA)或溶菌酶(LSZ)的磷酸盐缓冲盐水(PBS,pH 7.4)溶液中研究了奥氏体(AISI 304、310 和 316L)、铁素体(AISI 430)和双相(AISI 2205)等级的不锈钢的蛋白质诱导的金属释放。结果表明,BSA 和 LSZ 都会导致所有不锈钢等级表面氧化物中铬的显著富集。两种蛋白质都诱导了铁、铬、镍和锰的释放量显著增加,在 BSA 的情况下非常显著(增加了 40 倍),而两种蛋白质都降低了 SS 的耐腐蚀性,而铁金属则相反(存在蛋白质时,腐蚀速率降低,金属释放减少)。需要完全的单层覆盖才能诱导观察到的效果。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/1994b391c16f/10856_2013_4859_Fig10_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/0713c505bd4e/10856_2013_4859_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/9657f4bdfd75/10856_2013_4859_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/793dfff93796/10856_2013_4859_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/e997ad322f55/10856_2013_4859_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/ff32f7bbedb6/10856_2013_4859_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/16d420290c57/10856_2013_4859_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/c50bbe145257/10856_2013_4859_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/744e91d48d03/10856_2013_4859_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/f9bc3c4de408/10856_2013_4859_Fig9_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/1994b391c16f/10856_2013_4859_Fig10_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/0713c505bd4e/10856_2013_4859_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/9657f4bdfd75/10856_2013_4859_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/793dfff93796/10856_2013_4859_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/e997ad322f55/10856_2013_4859_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/ff32f7bbedb6/10856_2013_4859_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/16d420290c57/10856_2013_4859_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/c50bbe145257/10856_2013_4859_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/744e91d48d03/10856_2013_4859_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/f9bc3c4de408/10856_2013_4859_Fig9_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/51de/3620448/1994b391c16f/10856_2013_4859_Fig10_HTML.jpg

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