Literature DB >> 29745414

Ring structure modifications of phenylalanine 19 increase fibrillation kinetics and reduce toxicity of amyloid β (1-40).

Alexander Korn1, Dayana Surendran, Martin Krueger, Sudipta Maiti, Daniel Huster.   

Abstract

We investigated the influence of the chemical structure of the phenylalanine side chain in position 19 of the 40 residue amyloid β peptide. Side chain modifications in this position yielded fibrils of essentially unaltered morphology, structure, and dynamics, but significantly increased fibrillation kinetics and diminished the toxicity of the peptides.

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Year:  2018        PMID： 29745414     DOI： 10.1039/c8cc01733f

Source DB:  PubMed          Journal:  Chem Commun (Camb)        ISSN： 1359-7345            Impact factor:   6.222


  4 in total

1.  Repurposing Triphenylmethane Dyes to Bind to Trimers Derived from Aβ.

Authors:  Patrick J Salveson; Sepehr Haerianardakani; Alexander Thuy-Boun; Stan Yoo; Adam G Kreutzer; Borries Demeler; James S Nowick
Journal:  J Am Chem Soc       Date:  2018-09-06       Impact factor: 15.419

2.  Oxidation destabilizes toxic amyloid beta peptide aggregation.

Authors:  J Razzokov; M Yusupov; A Bogaerts
Journal:  Sci Rep       Date:  2019-04-02       Impact factor: 4.379

3.  Peptide backbone modifications of amyloid β (1-40) impact fibrillation behavior and neuronal toxicity.

Authors:  Benedikt Schwarze; Alexander Korn; Corinna Höfling; Ulrike Zeitschel; Martin Krueger; Steffen Roßner; Daniel Huster
Journal:  Sci Rep       Date:  2021-12-09       Impact factor: 4.379

4.  Probing the Influence of Single-Site Mutations in the Central Cross-β Region of Amyloid β (1-40) Peptides.

Authors:  Jacob Fritzsch; Alexander Korn; Dayana Surendran; Martin Krueger; Holger A Scheidt; Kaustubh R Mote; Perunthiruthy K Madhu; Sudipta Maiti; Daniel Huster
Journal:  Biomolecules       Date:  2021-12-09
  4 in total

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