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Self-assembled peptide amphiphiles function as multivalent binder with increased hemagglutinin affinity

机译:自组装肽两亲物可作为具有增加的血凝素亲和力的多价结合剂

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Background A promising way in diagnostic and therapeutic applications is the development of peptide amphiphiles (PAs). Peptides with a palmitic acid alkylchain were designed and characterized to study the effect of the structure modifications on self-assembling capabilities and the multiple binding capacity to hemagglutinin (HA), the surface protein of influenza virus type A. The peptide amphiphiles consists of a hydrophilic headgroup with a biological functionality of the peptide sequence and a chemically conjugated hydrophobic tail. In solution they self-assemble easily to micelles with a hydrophobic core surrounded by a closely packed peptide-shell. Results In this study the effect of a multiple peptide binding partner to the receptor binding site of HA could be determined with surface plasmon resonance measurements. The applied modification of the peptides causes signal amplification in relationship to the unmodified peptide wherein the high constant specificity persists. The molecular assembly of the peptides was characterized by the determination of critical micelle concentration (CMC) with concentration of 10-5 M and the colloidal size distribution. Conclusion The modification of the physico-chemical parameters by producing peptide amphiphiles form monomeric structures which enhances the binding affinity and allows a better examination of the interaction with the virus surface protein hemagglutinin.
机译:背景技术在诊断和治疗应用中有希望的方法是开发肽两亲物(PA)。设计并表征了具有棕榈酸烷基链的肽,以研究结构修饰对甲型流感病毒表面蛋白血凝素(HA)的自组装能力和多重结合能力的影响。该肽两亲物由亲水性组成具有肽序列的生物学功能的头基和化学缀合的疏水尾。在溶液中,它们易于自组装成带有疏水核并被紧密堆积的肽-壳包围的胶束。结果在本研究中,可以通过表面等离振子共振测量来确定多肽结合伴侣对HA受体结合位点的影响。肽的所施加的修饰引起与未修饰的肽相关的信号放大,其中未修饰的肽持续存在高恒定特异性。通过测定临界胶束浓度(CMC)(浓度为10 -5 M)和胶体大小分布来表征肽的分子组装。结论通过产生肽两亲物来改变理化参数形成单体结构,该单体结构增强了结合亲和力,并可以更好地检查与病毒表面蛋白血凝素的相互作用。

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