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Surface engineering: optimization of antigen presentation in self-assembled monolayers.

机译:表面工程:自组装单层中抗原呈递的优化。

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摘要

The formation of self-assembled monolayers (SAMs) on gold surfaces containing an antigenic peptide (NANP)6 and HS(CH2)11OH, and the specific binding of a monoclonal antibody to these layers were investigated by surface plasmon resonance (SPR). Peptides were synthesized by solid-state phase synthesis and were linked either to cysteine or to an alkyl-thiol to allow covalent attachment to gold. The content of the peptide in the SAMs was systematically varied, and the binding properties of the monoclonal antibody were compared with those measured by microcalorimetry in solution. At a critical peptide concentration in the SAM an optimal antibody binding and complete surface coverage was attained. At lower peptide concentrations, the amount of adsorbed antibody decreased; at higher peptide concentrations, the binding constant decreased. These effects can be explained if the accessibility of the antigenic epitopes depends on the peptide density. Addition of free antigen induced the desorption of bound antibodies and allowed accurate measurements of the dissociation rate constant. Binding constants obtained from steady-state measurements and from measurements of the kinetic rate constants were compared.
机译:通过表面等离振子共振(SPR)研究了含有抗原肽(NANP)6和HS(CH2)11OH的金表面上自组装单分子膜(SAMs)的形成,以及单克隆抗体与这些分子的特异性结合。通过固相合成法合成肽,并将其连接至半胱氨酸或烷基硫醇以使其与金共价连接。系统地改变SAM中肽的含量,并将单克隆抗体的结合特性与通过微量量热法在溶液中测得的结合特性进行比较。在SAM中的临界肽浓度下,可获得最佳的抗体结合和完全的表面覆盖。在较低的肽浓度下,抗体吸附量减少;在较高的肽浓度下,结合常数降低。如果抗原决定簇的可及性取决于肽密度,则可以解释这些效果。游离抗原的添加诱导结合的抗体的解吸,并允许精确测量解离速率常数。比较了从稳态测量和动力学速率常数的测量获得的结合常数。

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