Results 71 to 80 of about 75,180 (286)

Fibrillisation of hydrophobically modified amyloid peptide fragments in an organic solvent [PDF]

open access: yes, 2007
The self-assembly of a hydrophobically modified fragment of the amyloid beta(A beta) peptide has been studied in methanol. The peptide FFKLVFF is based on A beta(16-20) extended at the N terminus by two phenylalanine residues.
Castelletto, Valeria   +2 more
core   +1 more source

Aggregate Geometry in Amyloid Fibril Nucleation [PDF]

open access: yesPhysical Review Letters, 2013
We present and study a minimal structure-based model for the self-assembly of peptides into ordered beta-sheet-rich fibrils. The peptides are represented by unit-length sticks on a cubic lattice and interact by hydrogen bonding and hydrophobicity forces.
Irbäck, Anders   +4 more
openaire   +5 more sources

Towards Optimal Control of Amyloid Fibrillation

open access: yesBulletin of Mathematical Biology, 2023
26pages, 7 ...
Mengshou Wang   +3 more
openaire   +3 more sources

Kelvin Probe Force Microscopy in Bionanotechnology: Current Advances and Future Perspectives

open access: yesAdvanced Materials, EarlyView.
Kelvin probe force microscopy (KPFM) enables the nanoscale mapping of electrostatic surface potentials. While widely applied in materials science, its use in biological systems remains emerging. This review presents recent advances in KPFM applied to biological samples and provides a critical perspective on current limitations and future directions for
Ehsan Rahimi   +4 more
wiley   +1 more source

Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies

open access: yesCommunications Biology, 2021
Nguyen et al identified cytotoxic amyloid fibrils with oligomer-like characteristics, which were assembled from an islet amyloid polypeptide (IAPP) derivative containing an Asn-to-Gln substitution (N21Q). They presented evidence to show that these stable
Phuong Trang Nguyen   +5 more
doaj   +1 more source

Co-populated Conformational Ensembles of β(2)-Microglobulin Uncovered Quantitatively by Electrospray Ionization Mass Spectrometry [PDF]

open access: yes, 2004
Ordered assembly of monomeric human β(2)-microglobulin (β(2)m) into amyloid fibrils is associated with the disorder hemodialysis-related amyloidosis. Previously, we have shown that under acidic conditions (pH
Bjorkman   +46 more
core   +1 more source

Label‐Free SERS Fingerprinting of Neuroprotein Conformational Dynamics in Human Saliva

open access: yesAdvanced Materials, EarlyView.
Galvanic molecular entrapment (GME) is a label‐free method for detecting and quantifying neuroprotein conformational states. This technique enables direct surface binding and in situ hotspot generation around molecules, effectively overcoming challenges related to target localization and mismatched hotspot geometries.
Muhammad Shalahuddin Al Ja'farawy   +10 more
wiley   +1 more source

QBP1 Peptide as a Potential Anti‐Amyloidogenic Therapy for Type 2 Diabetes: An In Vitro Study

open access: yesAdvanced Science, EarlyView.
The anti‐amyloidogenic peptide QBP1 effectively halts human islet amyloid polypeptide (hIAPP) aggregation, preventing the formation of toxic β‐structured intermediates. Through a combination of biophysical assays, molecular dynamics, and cell‐based studies, QBP1 is shown to preserve β‐cell viability and metabolic homeostasis, positioning it as a ...
María M. Tejero‐Ojeda   +8 more
wiley   +1 more source

Nanomechanical Characterization of Apolipoprotein A-I Amyloid Fibrils

open access: yesEast European Journal of Physics, 2020
Amyloid fibrils represent a special type of protein aggregates that are currently receiving enormous attention due to their strong implication in molecular etiology of a wide range of human disorders.
Valeriya Trusova   +5 more
doaj   +1 more source

Food protein-derived amyloids do not accelerate amyloid β aggregation

open access: yesScientific Reports, 2023
The deposition of proteins in the form of amyloid fibrils is closely associated with several serious diseases. The events that trigger the conversion from soluble functional proteins into insoluble amyloid are not fully understood. Many proteins that are
M. Mahafuzur Rahman   +6 more
doaj   +1 more source

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