Amyloid-like Fibrils from a Diphenylalanine Capped with an Aromatic Fluorenyl,Langmuir

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Amyloid-like Fibrils from a Diphenylalanine Capped with an Aromatic Fluorenyl
Langmuir ( IF 3.7 ) Pub Date : 2018-11-19 00:00:00 , DOI: 10.1021/acs.langmuir.8b03378
Didac Martí _{1,

2} , Enric Mayans ₁ , Ana M. Gil ₃ , Angélica Díaz _{1,

2} , Ana I. Jiménez ₃ , Ibraheem Yousef ₄ , Ina Keridou _{1,

2} , Carlos Cativiela ₃ , Jordi Puiggalí _{1,

2} , Carlos Alemán _{1,

2}

Affiliation

The self-assembly behavior of a diphenylalanine amphiphile blocked at the C-terminus with a 9-fluorenylmethyl ester and stabilized at the N-terminus with a trifluoroacetate (TFA) anion, TFA·FF-OFm, has been examined. At low peptide concentration (0.5 mg/mL), long amyloid-like fibrils, which come from the fusion of two or more helical ribbons and/or thinner fibrils, organized in bundles or as individual entities are detected. Microbeam synchrotron radiation infrared spectroscopy has shown that TFA·FF-OFm molecules in amyloid-like fibrils arrange, forming antiparallel β-sheets. Alteration of the experimental conditions to prioritize the thermodynamic contribution with respect to the kinetic one in the self-assembly process inhibits the organization of amyloid-like structures in favor of the formation of conventional fibrous structures. On the basis of experimental observations, a structural model where the individual antiparallel β-sheets are oriented in parallel has been proposed for TFA·FF-OFm amyloid-like fibrils.

中文翻译：

来自二苯基丙氨酸的芳香族芴基封端的淀粉样蛋白原纤维

已经研究了二苯丙氨酸两亲物的自组装行为，该两性苯丙氨酸两亲物在C末端被9-芴基甲基酯封闭，并在N末端被三氟乙酸根（TFA）阴离子TFA·FF-OFm稳定。在低肽浓度（0.5 mg / mL）下，检测到长淀粉样样原纤维，它们是由两个或多个螺旋带和/或更薄的原纤维融合而成的，呈束状或以单个实体的形式存在。微束同步辐射红外光谱显示淀粉样样原纤维中的TFA·FF-OFm分子排列，形成反平行的β-折叠。在自组装过程中改变实验条件以相对于动力学优先考虑热力学贡献，从而抑制了淀粉样结构的组织，有利于常规纤维结构的形成。

更新日期：2018-11-19

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