Mechanical and thermodynamic properties of Aβ₄₂, Aβ₄₀, and α-synuclein fibrils: a coarse-grained method to complement experimental studies

• Adolfo B. Poma,
• Horacio V. Guzman,
• Mai Suan Li and
• Panagiotis E. Theodorakis

Beilstein J. Nanotechnol. 2019, 10, 500–513, doi:10.3762/bjnano.10.51

• formation. Finally, we find that α-synuclein fibrils are thermally less stable than β-amyloid fibrils. We anticipate that our molecular-level analysis of the mechanical response under different deformation conditions for the range of fibrils considered here will provide significant insights for the

• experimental observations. Keywords: β-amyloid; atomic force microscopy, mechanical deformation; molecular simulation; proteins; α-synuclein; Introduction All-atom molecular dynamics (MD) simulations have been employed to study the physical and chemical behaviour of the fundamental biomolecules of life (e.g

• investigate one α-synuclein and five β-amyloid fibrils of known experimental structure related to specific neurodegenerative diseases. Our simulation sheds light on the mechanical and thermodynamic properties of these fibrils by providing the microscopic picture required to explain the relevant phenomena. We

Strategy to discover full-length amyloid-beta peptide ligands using high-efficiency microarray technology

• Clelia Galati,
• Natalia Spinella,
• Lucio Renna,
• Danilo Milardi,
• Francesco Attanasio,
• Michele Francesco Maria Sciacca and
• Corrado Bongiorno

Beilstein J. Nanotechnol. 2017, 8, 2446–2453, doi:10.3762/bjnano.8.243

• Abstract Although the formation of β-amyloid (Aβ) fibrils in neuronal tissues is a hallmark of Alzheimer disease (AD), small-sized Aβ oligomers rather than mature fibrils have been identified as the most neurotoxic species. Therefore, the design of new inhibitors, able to prevent the aggregation of Aβ, is

• mid-1990’s presented the KLVFF pentapeptide (Aβ16–20) as a strategy to arrest the formation of β-amyloid fibrils, confirming that amino-acid residues located within or close to this region are important for the adoption of the correct β-sheet structure of Aβ [30]. Semax is an hexapeptide (Met–Glu–His

Straightforward and robust synthesis of monodisperse surface-functionalized gold nanoclusters

• Silvia Varela-Aramburu,
• Richard Wirth,
• Chian-Hui Lai,
• Guillermo Orts-Gil and
• Peter H. Seeberger

Beilstein J. Nanotechnol. 2016, 7, 1278–1283, doi:10.3762/bjnano.7.118

• carbohydrates [13], proteins [14], antibodies [15] and DNA [16] are commonly used as multivalent materials for biological studies. Gold nanoparticles have been used in vivo as radiotracers [15][17], for targeted delivery [18] and, when functionalized with carboxylic acids, inhibit β-amyloid fibril growth