Premium
Cover Feature: The Impact of Halogenated Phenylalanine Derivatives on NFGAIL Amyloid Formation (ChemBioChem 24/2020)
Author(s) -
Chowdhary Suvrat,
Moschner Johann,
Mikolajczak Dorian J.,
Becker Maximilian,
Thünemann Andreas F.,
Kästner Claudia,
Klemczak Damian,
Stegemann AnneKatrin,
Böttcher Christoph,
Metrangolo Pierangelo,
Netz Roland R.,
Koksch Beate
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202000779
Subject(s) - kinetics , folding (dsp implementation) , chemistry , amyloid fibril , amyloid (mycology) , phenylalanine , protein folding , peptide , fibril , biophysics , stereochemistry , amyloid β , biochemistry , amino acid , biology , physics , inorganic chemistry , engineering , medicine , disease , pathology , quantum mechanics , electrical engineering
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.