Impact on the replacement of Phe by Trp in a short fragment of Aβ amyloid peptide on the formation of fibrils

No abstract is available for this paper.

• Publication year

  2011

• Venue

  Journal of Peptide Science

• Publication date

  2011-02-01

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1002/psc.1339PMID 21234983
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Probing the amyloid-beta(1-40) fibril environment with substituted tryptophan residues.

  2010cited by this paper
• Aromatic-aromatic interactions induce the self-assembly of pentapeptidic derivatives in water to form nanofibers and supramolecular hydrogels.

  2010cited by this paper
• pH controlled aggregation morphology of Abeta(16-22): formation of peptide nanotubes, helical tapes and amyloid fibrils.

  2009cited by this paper
• Morphology of self‐assembled structures formed by short peptides from the amyloidogenic protein tau depends on the solvent in which the peptides are dissolved

  2009cited by this paper
• Organic solvent mediated self‐association of an amyloid forming peptide from β2‐microglobulin: An atomic force microscopy study

  2008cited by this paper
• Self-assembly and hydrogelation of an amyloid peptide fragment.

  2008cited by this paper
• Facial symmetry in protein self-assembly.

  2008cited by this paper
• Cross-strand pairing and amyloid assembly.

  2008cited by this paper
• Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology.

  2007cited by this paper
• Fibrillisation of hydrophobically modified amyloid peptide fragments in an organic solvent.

  2007cited by this paper
• Atomic structures of amyloid cross-β spines reveal varied steric zippers

  2007cited by this paper
• Atomic structures of amyloid cross-beta spines reveal varied steric zippers.

  2007cited by this paper
• Peptide fibrillization.

  2007cited by this paper
• A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments.

  2006cited by this paper
• Designed aromatic homo-dipeptides: formation of ordered nanostructures and potential nanotechnological applications

  2006cited by this paper
• A systematic screen of β2-microglobulin and insulin for amyloid-like segments

  2006cited by this paper
• Experimental evidence for the reorganization of beta-strands within aggregates of the Abeta(16-22) peptide.

  2005cited by this paper
• Experimental Evidence for the Reorganization of β-Strands within Aggregates of the Aβ(16−22) Peptide

  2005cited by this paper
• Mechanisms of amyloid fibril self‐assembly and inhibition

  2005cited by this paper
• Role of aromatic interactions in amyloid formation by peptides derived from human Amylin.

  2004cited by this paper
• The Formation of Straight and Twisted Filaments from Short Tau Peptides*

  2004cited by this paper
• Oligomerization of amyloid Abeta16-22 peptides using hydrogen bonds and hydrophobicity forces.

  2004cited by this paper
• Dissecting the assembly of Abeta16-22 amyloid peptides into antiparallel beta sheets.

  2003cited by this paper
• Short peptide amyloid organization: stabilities and conformations of the islet amyloid peptide NFGAIL.

  2003cited by this paper
• Completely different amyloidogenic potential of nearly identical peptide fragments.

  2003cited by this paper
• Exploiting amyloid fibril lamination for nanotube self-assembly.

  2003cited by this paper
• Casting Metal Nanowires Within Discrete Self-Assembled Peptide Nanotubes

  2003cited by this paper
• Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro.

  2003cited by this paper
• Supramolecular Structure in Full-Length Alzheimer's β-Amyloid Fibrils: Evidence for a Parallel β-Sheet Organization from Solid-State Nuclear Magnetic Resonance

  2002cited by this paper
• Stabilities and conformations of Alzheimer's beta -amyloid peptide oligomers (Abeta 16-22, Abeta 16-35, and Abeta 10-35): Sequence effects.

  2002cited by this paper
• Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance.

  2002cited by this paper
• A possible role for π‐stacking in the self‐assembly of amyloid fibrils

  2002cited by this paper
• Amyloid Fibril Formation by Pentapeptide and Tetrapeptide Fragments of Human Calcitonin*

  2002cited by this paper
• Stabilities and conformations of Alzheimer's β-amyloid peptide oligomers (Aβ16–22, Aβ16–35, and Aβ10–35): Sequence effects

  2002cited by this paper
• An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid

  2001cited by this paper
• C-H...pi Interactions in Proteins: A Structural Bioinformatics Study

  2001cited by this paper
• C-h⋯π-interactions in proteins

  2001cited by this paper
• Analysis of the Minimal Amyloid-forming Fragment of the Islet Amyloid Polypeptide

  2001cited by this paper
• Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR†

  2000cited by this paper
• Peptide Conformations in Alcohol and Water: Analyses by the Reference Interaction Site Model Theory

  2000cited by this paper
• Hydrophobic clustering in acid-denatured IL-2 and fluorescence of a Trp NH-pi H-bond.

  2000cited by this paper
• Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR.

  2000cited by this paper
• Aromatic interactions in homeodomains contribute to the low quantum yield of a conserved, buried tryptophan

  2000cited by this paper
• Medin: an integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid.

  1999cited by this paper
• A Molecular Model of Alzheimer Amyloid β-Peptide Fibril Formation*

  1999cited by this paper
• Amyloid beta.

  1999cited by this paper
• Molecular simulation of the effects of alcohols on peptide structure.

  1999cited by this paper
• pi-Stacking interactions. Alive and well in proteins.

  1998cited by this paper
• Amyloid, the presenilins and Alzheimer's disease.

  1997cited by this paper
• π–π INTERACTIONS IN SELF‐ASSEMBLY

  1997cited by this paper
• Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment.

  1993cited by this paper
• The N-terminal segment of protein AA determines its fibrillogenic property.

  1992cited by this paper
• pH-dependent structural transitions of Alzheimer amyloid peptides.

  1991cited by this paper
• A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis.

  1990cited by this paper
• Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic beta-protein fragments.

  1990cited by this paper
• Amino‐aromatic interactions in proteins

  1986cited by this paper
• Aromatic-aromatic interaction: a mechanism of protein structure stabilization.

  1985cited by this paper
• Time-resolved fluorescence of proteins.

  1985cited by this paper

• De novo designed aliphatic and aromatic peptides assemble into amyloid-like cytotoxic supramolecular nanofibrils

  2024cites this paper
• Phenylalanine-based fibrillar systems.

  2023cites this paper
• Molecular mechanisms of resveratrol and EGCG in the inhibition of Aβ42 aggregation and disruption of Aβ42 protofibril: similarities and differences.

  2021cites this paper
• Nano‐Assemblies of a Synthetic Peptide: Illuminating Aggregation Potential, Amyloidogenicity and Cytotoxicity

  2021cites this paper
• Hydrogel Formation by an Aromatic Analogue of a β-Amyloid Fragment, Aβ16–22: A Scaffold for 3D Cell Culture

  2019cites this paper
• Interaction of cavin-1/PTRF leucine zipper domain 2 and its congenital generalized lipodystrophy mutant with model membranes.

  2019cites this paper
• Bactericidal Potency and Extended Serum Life of Stereo-Chemically Engineered Peptides Against Mycobacterium

  2019cites this paper
• Peptido-mimetic Approach in the Design of Syndiotactic Antimicrobial Peptides

  2018cites this paper
• Self‐assembly of β‐turn motif‐connected tandem repeats of Aβ16‐22 and its aromatic analogs

  2018cites this paper
• Effect of tacticity-derived topological constraints in bactericidal peptides.

  2017cites this paper
• Inhibition of peptide aggregation by means of enzymatic phosphorylation

  2016cites this paper
• Self‐assembly of a peptide with a tandem repeat of the Aβ16‐22 sequence linked by a β turn‐promoting dipeptide sequence

  2015cites this paper
• Probing the role of aromatic residues in the self-assembly of Aβ(16–22) in fluorinated alcohols and their aqueous mixtures

  2015cites this paper
• Effects of hydroxylated carbon nanotubes on the aggregation of Aβ16-22 peptides: a combined simulation and experimental study.

  2014cites this paper
• Self-assembly of Cu(II) with amyloid β19–20 peptide: relevant to Alzheimer's disease

  2014cites this paper
• Peptide self-assembly: from toxins to amyloid fibrils and nanotubes.

  2014cites this paper
• Amyloid Peptide Self-Assembly in Protic Ionic Liquids

  2013cites this paper
• Analysis of Amyloid Nanostructures Using Photo-cross-linking: In Situ Comparison of Three Widely Used Photo-cross-linkers

  2013cites this paper
• Aβ(16-22) peptides can assemble into ordered β-barrels and bilayer β-sheets, while substitution of phenylalanine 19 by tryptophan increases the population of disordered aggregates.

  2013cites this paper
• Hexafluoroisopropanol induces self‐assembly of β‐amyloid peptides into highly ordered nanostructures

  2012cites this paper
• Structural heterogeneities of self-assembled peptide nanomaterials

  2012cites this paper
• Phase networks of cross-β peptide assemblies.

  2012cites this paper
• Role of Cation in Enhancing the Conversion of the Alzheimer’s Peptide into Amyloid Fibrils Using Protic Ionic Liquids

  2012cites this paper
• Self‐assembly of short peptides composed of only aliphatic amino acids and a combination of aromatic and aliphatic amino acids

  2012cites this paper