具有抗非特异性蛋白质吸附能力的新型叔胺氧化物表面。

Novel tertiary amine oxide surfaces that resist nonspecific protein adsorption.

作者信息

Dilly Suzanne J, Beecham Matthew P, Brown Steven P, Griffin John M, Clark Andrew J, Griffin Craig D, Marshall Jacqueline, Napier Richard M, Taylor Paul C, Marsh Andrew

机构信息

Department of Chemistry, University of Warwick, Coventry, UK.

出版信息

Langmuir. 2006 Sep 12;22(19):8144-50. doi: 10.1021/la060743j.

DOI:10.1021/la060743j

PMID:16952254

Abstract

Novel surfaces derivatized with tertiary amine oxides have been prepared and tested for their ability to resist nonspecific protein adsorption. The oxidation of tertiary amines supported on triazine units was carried out using mCPBA to give a format allowing conjugation of biologically active ligands alongside them. Adsorption to these surfaces was tested and compared to adsorption to a set of commercial and custom oligo-/poly(ethylene glycol) (OEG/PEG) supports by challenging them with a protein display library presented on bacteriophage lambda. The new class of amine oxide surfaces is found to compare favorably with the performance of the OEG/PEG supports in the prevention of nonspecific binding.

摘要

已制备了用叔胺氧化物衍生化的新型表面，并测试了它们抵抗非特异性蛋白质吸附的能力。使用间氯过氧苯甲酸对三嗪单元上负载的叔胺进行氧化，以得到一种形式，使生物活性配体能够与它们共轭。测试了蛋白质在这些表面上的吸附情况，并通过用噬菌体λ展示的蛋白质文库对其进行挑战，将其与一系列商业和定制的寡聚/聚（乙二醇）（OEG/PEG）载体上的吸附情况进行了比较。发现新型叔胺氧化物表面在防止非特异性结合方面的性能与OEG/PEG载体相当。