Literature DB >> 32199918

Role of aromatic amino acids in amyloid self-assembly.

Ivana M Stanković1, Shuqiang Niu2, Michael B Hall2, Snežana D Zarić3.   

Abstract

Amyloids are proteins of a cross-β structure found as deposits in several diseases and also in normal tissues (nails, spider net, silk). Aromatic amino acids are frequently found in amyloid deposits. Although they are not indispensable, aromatic amino acids, phenylalanine, tyrosine and tryptophan, enhance significantly the kinetics of formation and thermodynamic stability, while tape or ribbon-like morphology is represented in systems with experimentally detected π-π interactions between aromatic rings. Analysis of geometries and energies of the amyloid PDB structures indicate the prevalence of aromatic-nonaromatic interactions and confirm that aromatic-aromatic interactions are not crucial for the amyloid formation.
Copyright © 2020. Published by Elsevier B.V.

Entities:  

Keywords:  Amyloids; Aromatic amino acids; Self-assembly

Mesh:

Substances:

Year:  2020        PMID: 32199918     DOI: 10.1016/j.ijbiomac.2020.03.064

Source DB:  PubMed          Journal:  Int J Biol Macromol        ISSN: 0141-8130            Impact factor:   6.953


  7 in total

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6.  1,3,5-Triazine Nitrogen Mustards with Different Peptide Group as Innovative Candidates for AChE and BACE1 Inhibitors.

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7.  Capacity for increased surface area in the hydrophobic core of β-sheet peptide bilayer nanoribbons.

Authors:  Christopher W Jones; Crystal G Morales; Sharon L Eltiste; Francine E Yanchik-Slade; Naomi R Lee; Bradley L Nilsson
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  7 in total

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