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Growth, Polymorphism, and Spatially Controlled Surface Immobilization of Biotinylated Variants of IAPP21-27 Fibrils.
Biomacromolecules ( IF 5.5 ) Pub Date : 2020-01-22 , DOI: 10.1021/acs.biomac.9b01466
Torsten John 1, 2 , Juhaina Bandak 1 , Nilushiya Sarveson 1 , Claudia Hackl 1 , Herre Jelger Risselada 1, 3 , Andrea Prager 1 , Christian Elsner 1 , Bernd Abel 1, 2
Affiliation  

The islet amyloid polypeptide (IAPP) is a regulatory peptide that can aggregate into fibrillar structures associated with type 2 diabetes. In this study, the IAPP21-27 segment was modified with a biotin linker at the N-terminus (Btn-GNNFGAIL) to immobilize peptide fibrils on streptavidin-coated surfaces. Key residues for fibril formation of the N-terminal biotinylated IAPP21-27 segment were identified by using an alanine scanning approach combined with molecular dynamics simulations, thioflavin T fluorescence measurements, and scanning electron microscopy. Significant contributions of phenylalanine (F23), leucine (L27), and isoleucine (I26) for the fibrillation of the short peptide segment were identified. The fibril morphologies of the peptide variants differed depending on their primary sequence, ranging from flexible and semiflexible to stiff and crystal-like structures. These insights could advance the design of new functional hybrid bionanomaterials and fibril-engineered surface coatings using short peptide segments. To validate this concept, the biotinylated fibrils were immobilized on streptavidin-coated surfaces under spatial control.

中文翻译:

IAPP21-27原纤维生物素化变体的生长,多态性和空间控制的表面固定化。

胰岛淀粉样多肽(IAPP)是一种调节肽,可以聚集到与2型糖尿病相关的原纤维结构中。在这项研究中,使用生物素接头在N端(Btn-GNNFGAIL)修饰了IAPP21-27片段,以将肽原纤维固定在链霉亲和素包被的表面上。N端生物素化的IAPP21-27节的原纤维形成的关键残基是通过使用丙氨酸扫描方法结合分子动力学模拟,硫黄素T荧光测量和扫描电子显微镜确定的。鉴定了苯丙氨酸(F23),亮氨酸(L27)和异亮氨酸(I26)对短肽段的原纤化的重要贡献。肽变体的原纤维形态取决于其一级序列,从柔韧性和半柔韧性到坚硬的晶体状结构。这些见解可以推动使用短肽段的新型功能性杂合纳米材料和原纤维工程化表面涂层的设计。为了验证该概念,在空间控制下将生物素化的原纤维固定在链霉亲和素包被的表面上。
更新日期:2020-01-23
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