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- W2037441567 abstract "Aromatic amino acids have been suspected to drive the aggregation mechanism in amyloidogenic peptides by virtue of their hydrophobicity and aromaticity. Alzheimer's disease in particular is associated with the aggregation of a 39-42 residue polypeptide (Amyloid β, Aβ) and its subsequent deposition into amyloid plaques. The aromatic phenylalanine residues (Phe19 and Phe20) in the central hydrophobic cluster (CHC) of the peptide have been suspected to play a significant role in such aggregation. In the present study the amyloid β 10-35 (Aβ10-35) fragment has been used as a model system, where the CHC has been perturbed through the introduction of non-natural amino acids. We have prepared variants where Phe19 and Phe20 have been systematically replaced by pentafluorophenylalanine (F5-Phe) and their affect on amyloid aggregation and kinetics has been studied by biophysical techniques including circular dichroism (CD), fluorescence, UV resonance Raman (UVRR) spectroscopy and chemometrics. While Phe→F5-Phe mutations have been found to enhance conformational stability in Aβ16-22 (Senguen et al. Mol. BioSyst., 2011, 7, p486) by virtue of enhanced hydrophobicity, unfavorable steric interactions brought about by such substitution can also lead to destabilization in some systems (Cornilescu et al., Prot.Sc., 2007, 16, p14). Our experimental studies show that aggregation in both the wild type (wT) Aβ10-35 and the Phe 19→F5-Phe mutant proceeds via a two step conformational transition pathway (wTAβ10-35: T1= 9.18 ±1.4 hrs, T2= 9.79 ±0.44 days, F5-Phe19: T1= 10.72 ± 2.1 hrs, T2= 7.6 ± 0.47 days). However the Phe 20→F5-Phe mutants fail to aggregate into β-sheets as confirmed by both CD and fluorescence studies. Deep UVRR studies have also been performed to probe the fibrillation process and monitor the structural changes brought about by the F5-Phe substitution and their effect on amyloid aggregation." @default.
- W2037441567 created "2016-06-24" @default.
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- W2037441567 date "2013-01-01" @default.
- W2037441567 modified "2023-09-29" @default.
- W2037441567 title "Modulating Amyloid Aggregation by Incorporation of Fluorinated Phenylalanine Derivatives in the Central Hydrophobic Cluster of Aβ10-35" @default.
- W2037441567 doi "https://doi.org/10.1016/j.bpj.2012.11.299" @default.
- W2037441567 hasPublicationYear "2013" @default.
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