Tethering Hydrophobic Peptides to Functionalized Self-Assembled Mono layers on Gold through Two Chemical Linkers Using the Huisgen Cycloaddition
Tethering Hydrophobic Peptides to Functionalized Self-Assembled Mono layers on Gold through Two Chemical Linkers Using the Huisgen Cycloaddition
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DOI：
10.1021/la1036585
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发表时间：
2010-12-21
期刊：
影响因子：
3.9
通讯作者：
Webb, Lauren J.
中科院分区：
文献类型：
--
作者：
Gallardo, Ignacio F.;Webb, Lauren J.
用α-螺旋肽官能化的金表面已经通过使叠氮化物封端的自组装单层与含有两个氰基苯丙氨酸的结构化肽通过Huisgen环加成反应而产生。反应性溴封端的硫醇和惰性烷硫醇的混合单层制备在各种浓度的Br-封端的部分。这些与叠氮化钠反应，形成叠氮化物封端的单层与控制浓度的反应性叠氮化物。这些表面进行了研究，通过椭圆偏振和X射线光电子能谱，这表明，在表面上的反应性叠氮基团的浓度是由化学条件下，单层制备控制。叠氮化物封端表面的掠入射角表面红外光谱（GRAS-IR）表明，叠氮化物大致垂直于表面的平面，正如预期的那样。然后将这些表面暴露于由交替的亮氨酸和赖氨酸残基组成的α-螺旋肽，其中两个残基被氰基苯丙氨酸取代以与两个相邻的表面结合的叠氮基反应，从而通过两个共价键将肽结合到表面。通过GRAS-IR监测叠氮基团的吸收来定量该反应的产率。尽管在反应期间对单分子膜造成损伤，但在优化的反应条件下，反应产率为80-98%。虽然肽保留其α-螺旋构型下的反应条件下，GRAS-IR分析的酰胺I和II模式的表面结合的肽表明，它可能是随机取向的表面上。
Gold surfaces functionalized with an a-helical peptide have been generated by reacting an azide-terminated self-assembled monolayer with structured peptides containing two cyanophenylalanines through a Huisgen cycloaddition. Mixed monolayers of a reactive bromine-terminated thiol and inert alkane thiol were prepared at various concentrations of the Br-terminated moiety. These were reacted with sodium azide to form azide-terminated monolayers with controlled concentration of the reactive azide. These surfaces were studied through ellipsometry and X-ray photoelectron spectroscopy, which demonstrated that the concentration of the reactive azide group on the surface is controlled by the chemical conditions under which the monolayer is prepared. Grazing incident angle surface infrared spectroscopy (GRAS-IR) of the azide-terminated surface demonstrated that the azide is approximately perpendicular to the plane of the surface, as expected. These surfaces were then exposed to an a-helical peptide composed of alternating leucine and lysine residues, with two residues replaced with cyanophenylalanine to react with two neighboring surface-bound azide groups to bind the peptide to the surface through two covalent bonds. The yield of this reaction was quantified through monitoring the absorption of the azide group by GRAS-IR. Despite damage to the monolayer during the reaction, reaction yields of 80-98% were determined for optimized reaction conditions. Although the peptide retains its a-helical configuration under the reaction conditions, GRAS-IR analysis of the amide I and II modes of the surface-bound peptide showed that it is probably randomly oriented on the surface.