Self-assembly and adhesive properties of Pollicipes pollicipes barnacle cement protein cp19k: influence of pH and ionic strength

• Shrutika Sawant,
• Anne Marie Power and
• J. Gerard Wall

Beilstein J. Nanotechnol. 2025, 16, 1863–1872, doi:10.3762/bjnano.16.129

• to promote the formation of extended, needle-like fibrils by the cp19k protein. The β-amyloid nature of fibrils formed under these conditions and at high pH/low salt concentration was confirmed by Thioflavin T assay. Non-fibrillar cp19k adhered most effectively to hydrophilic and hydrophobic surfaces

• rPolcp19k-his protein samples that had been incubated at pH 8.0 with no NaCl, followed by rPolcp19k-his at pH 4.0 and 600 mM NaCl or 150 mM NaCl (Figure 3). This is indicative of the occurrence of β-amyloid in the samples and, combined with the TEM analysis (Figure 1 and Figure 2), indicates that the cp19k

• environment as optimal for formation of β-amyloid-containing fibrils by recombinant P. pollicipes cp19k (rPpolcp19k). We hypothesise that these conditions reflect the acidic, iso-osmotic environment of the adhesive glands in P. pollicipes, an open-coast species adapted to full-strength seawater. The different

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