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Cover Feature: The Impact of Halogenated Phenylalanine Derivatives on NFGAIL Amyloid Formation (ChemBioChem 24/2020)
ChemBioChem ( IF 2.6 ) Pub Date : 2020-11-27 , DOI: 10.1002/cbic.202000779
Suvrat Chowdhary 1 , Johann Moschner 1 , Dorian J. Mikolajczak 1 , Maximilian Becker 2 , Andreas F. Thünemann 3 , Claudia Kästner 3 , Damian Klemczak 4 , Anne‐Katrin Stegemann 1 , Christoph Böttcher 5 , Pierangelo Metrangolo 6 , Roland R. Netz 2 , Beate Koksch 1
Affiliation  

As shown for the model peptide NFGAIL, the introduction of different fluorinated phenylalanine derivatives leads to specific amyloid‐folding kinetics through an alteration in hydrophobicity and changes in their α‐frameworks. This is represented by the clock, as its hand (the “F” for fluorine) determines the self‐assembly process. The extent of fluorination, illustrated as potential plots, acts as a dimension of change not only for aggregation kinetics, but also for the morphology of resulting fibrils, as revealed by TEM micrographs. More information can be found in the full paper by B. Koksch et al. The picture was created by S.C., Helmut Fouquet, J.M., M.B., R.R.N. and B.K.
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中文翻译:

封面人物:卤代苯丙氨酸衍生物对NFGAIL淀粉样蛋白形成的影响(ChemBioChem 24/2020)

如模型肽NFGAIL所示,引入不同的氟化苯丙氨酸衍生物可通过改变疏水性和改变其α构架而导致特定的淀粉样蛋白折叠动力学。这由时钟表示,因为它的指针(氟的“ F”)决定了自组装过程。如电势图所示,氟化程度不仅是聚集动力学的变化维度,而且是所得原纤维形态的变化维度,如TEM显微照片所示。B. Koksch等人在全文中可以找到更多信息。图片是由SC,Helmut Fouquet,JM,MB,RRN和BK创建的
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更新日期:2020-12-12
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