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疏水蛋白可以防止蛋白质在疏水基底上的二次吸附，而无需进行交换。

Hydrophobin can prevent secondary protein adsorption on hydrophobic substrates without exchange.

机构信息

Polymer Physics, BASF SE, Carl-Bosch-Str. 38, 67056, Ludwigshafen, Germany.

出版信息

Anal Bioanal Chem. 2011 Jun;400(7):2031-40. doi: 10.1007/s00216-011-4902-x. Epub 2011 Apr 5.

DOI:10.1007/s00216-011-4902-x
PMID:21461987
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3098362/
Abstract

By combining several surface analytical tools, we show that an adsorbed layer of the protein HProtein B prevents the adsorption of secondary proteins bovine serum albumin, casein, or collagen at low-salinity conditions and at pH 8. HProtein B is an industrially producible fusion protein of the hydrophobin family, known for its high interfacial activity. While applications of hydrophobin have been reported to facilitate adhesion of proteins under different pH conditions, careful analysis by quartz-crystal microbalance and ellipsometry prove that no additional adsorption can be found on top of the H*Protein B layer in this study. Surface analysis by X-ray photoelectron spectroscopy and secondary ion mass spectrometry proves that the hydrophobin layer stays intact even after hours of exposure to solutions of the secondary proteins and that no exchange of proteins can be detected.

摘要

通过结合几种表面分析工具，我们表明，在低盐度条件下和 pH8 时，蛋白质 HProtein B 的吸附层可以防止二级蛋白质牛血清白蛋白、酪蛋白或胶原蛋白的吸附。HProtein B 是一种可工业化生产的疏水蛋白家族融合蛋白，以其高界面活性而闻名。尽管已有报道称疏水蛋白的应用可以促进不同 pH 条件下蛋白质的粘附，但通过石英晶体微天平和椭偏仪的仔细分析证明，在本研究中，在 H*Protein B 层之上没有发现额外的吸附。X 射线光电子能谱和二次离子质谱的表面分析证明，即使在数小时暴露于二级蛋白质溶液中，疏水蛋白层仍保持完整，并且没有检测到蛋白质的交换。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/8a4cad70d50d/216_2011_4902_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/98df9f010a37/216_2011_4902_Figa_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/ee812d8a0498/216_2011_4902_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/36b930e37f54/216_2011_4902_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/5923949f23d0/216_2011_4902_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/56e5792c588f/216_2011_4902_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/d15b946a80d0/216_2011_4902_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/81b36a737e82/216_2011_4902_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/8a4cad70d50d/216_2011_4902_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/98df9f010a37/216_2011_4902_Figa_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/ee812d8a0498/216_2011_4902_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/36b930e37f54/216_2011_4902_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/5923949f23d0/216_2011_4902_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/56e5792c588f/216_2011_4902_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/d15b946a80d0/216_2011_4902_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/81b36a737e82/216_2011_4902_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/242e/3098362/8a4cad70d50d/216_2011_4902_Fig7_HTML.jpg

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Langmuir. 2010 May 4;26(9):6494-502. doi: 10.1021/la9039557.
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Surface modification using a novel type I hydrophobin HGFI.使用新型I型疏水蛋白HGFI进行表面改性。
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The Arthroderma benhamiae hydrophobin HypA mediates hydrophobicity and influences recognition by human immune effector cells.皮炎外瓶霉疏水蛋白HypA介导疏水性并影响人类免疫效应细胞的识别。
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