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Related papers: Amyloid Fibril Solubility

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The mineralized collagen fibril is the main building block of hard tissues and it directly affects the macroscopic mechanics of biological tissues such as bone. The mechanical behavior of the fibril itself is determined by its structure:…

Tissues and Organs · Quantitative Biology 2024-03-19 Julia Kamml , Claire Acevedo , David Kammer

Functional amyloid fibrils, once primarily associated with amyloidosis, are now recognized for their exceptional potential as biomaterials due to their unique structural features, including remarkable mechanical strength, high stability,…

Biomolecules · Quantitative Biology 2025-04-23 Shayan Mortazavi , Mehrnoosh Neshatian , Laurent Bozec , Hadis Zarrin , Mahshid Kalani

Polypeptides can self-assemble into hierarchically organized fibrils consisting of a stack of individually folded polypeptides driven together by hydrophobic interaction. Using a coarse grained model, we systematically studied this…

Soft Condensed Matter · Physics 2013-07-31 Ran Ni , Sanne Abeln , Marieke Schor , Martien A. Cohen Stuart , Peter G. Bolhuis

Protein oligomers have been implicated as toxic agents in a wide range of amyloid-related diseases. Yet it has remained unsolved whether the oligomers are a necessary step in the formation of amyloid fibrils, or just a dangerous by-product.…

Biomolecules · Quantitative Biology 2014-12-03 Anđela Šarić , Yassmine C. Chebaro , Tuomas P. J. Knowles , Daan Frenkel

Formation of amyloid fibrils of various amyloidogenic proteins is dramatically enhanced by ultrasound irradiation. For applying this phenomenon to the study of protein aggregation science and diagnosis of neurodegenerative diseases, a…

Rigidity analysis using the "pebble game" can usefully be applied to protein crystal structures to obtain information on protein folding, assembly and the structure-function relationship. However, previous work using this technique has not…

Molecular Networks · Quantitative Biology 2009-09-25 Stephen A. Wells , J. Emilio Jimenez-Roldan , Rudolf A. Römer

Amyloid fibrils are stable aggregates of misfolded proteins and polypeptides that are insoluble and resistant to protease activity. Abnormal formation of amyloid fibrils in vivo may lead to neurodegenerative disorders and other systemic…

Biomolecules · Quantitative Biology 2018-05-22 Boris Haimov , Simcha Srebnik

We propose an exactly solvable simplified statistical mechanical model for the thermodynamics of beta-amyloid aggregation, generalizing a well-studied model for protein folding. The monomer concentration is explicitly taken into account as…

Biomolecules · Quantitative Biology 2010-10-22 Marco Zamparo , Antonio Trovato , Amos Maritan

The need to understand the assembly kinetics of fibril formation has become urgent because of the realization that soluble oligomers of amyloidogenic peptides may be even more neurotoxic than the end product, namely, the amyloid fibrils. In…

Biomolecules · Quantitative Biology 2007-05-23 Ruxandra I. Dima , Bogdan Tarus , John E. Straub , D. Thirumalai

Conformation of a protein (CorA) is examined in a matrix with mobile solute constituents as a function of solute-residue interaction strength (f) by a coarse-grained model with a Monte Carlo simulation. Solute particles are found to reach…

Biological Physics · Physics 2020-08-26 Warin Rangubpit , Sunan Kitjaruwankul , Pornthep Sompornpisut , R. B. Pandey

The molecular distributions obtained from canonical Monte Carlo simulations can be used to find an approximate interaction energy. This serves as the basis of a method for estimating the binding free energy for a ligand to a protein which…

Chemical Physics · Physics 2007-05-23 Charles F. F. Karney , Jason E. Ferrara , Clay D. Spence

The mechanical properties of collagen fibrils depend on the amount and the distribution of water molecules within the fibrils. Here, we use atomic force microscopy (AFM) to study the effect of hydration on the viscoelastic properties of…

Soft Condensed Matter · Physics 2019-10-03 Manuel R. Uhlig , Robert Magerle

Collagen fibrils are the building block of many biological tissues, which viability depend on the fibrils properties. Altered properties of collagen fibrils are central to the appearance of many diseases, while physiological or native…

Soft Condensed Matter · Physics 2026-05-08 Konstantinos Steiakakis , Alan Pichard , Maxime Vassaux

Collagenolytic degradation is a process fundamental to tissue remodeling. The microarchitecture of collagen fibril networks changes during development, aging, and disease. Such changes to microarchitecture are often accompanied by changes…

Biological Physics · Physics 2024-08-13 B. Debnath , B. N. Narasimhan , S. I. Fraley , P. Rangamani

Mineralized collagen microfibrils in human bone provide its mechanical properties (stiffness, elasticity, ductility, energy dissipation and strength). However, detailed 3D finite element models describing the mechanical behaviour of the…

Tissues and Organs · Quantitative Biology 2012-03-01 Ridha Hambli , Abdelwahed Barkaoui

Dynamic bonding is an essential feature of many soft materials. Molecular simulations have proven to be a powerful tool for modeling bonding kinetics and thermodynamics in these materials, providing insights into their properties that…

Soft Condensed Matter · Physics 2026-05-26 Tyla R. Holoman , B. P. Prajwal , Glen M. Hocky , Thomas M. Truskett

Using atomic force microscopy (AFM) we investigated the interaction of amyloid beta (Ab) (1 42) peptide with chemically modified surfaces in order to better understand the mechanism of amyloid toxicity, which involves interaction of amyloid…

Biological Physics · Physics 2017-04-28 Brad Moores , Elizabeth Drolle , Simon Attwood , Janet Simons , Zoya Leonenko

Bone is mineralized tissue constituting the skeletal system, supporting and protecting body organs and tissues. At the molecular level, mineralized collagen fibril is the basic building block of bone tissue, and hence, understanding bone…

Atomic and Molecular Clusters · Physics 2021-06-16 Mario Milazzo , Alessio David , Gang Seob Jung , Serena Danti , Markus J. Buehler

Using exhaustive Monte Carlo simulations we study the kinetics and mechanism of fibril formation using lattice models as a function of temperature and the number of chains. While these models are, at best, caricatures of peptides, we show…

Biomolecules · Quantitative Biology 2009-11-13 Mai Suan Li , D. K. Klimov , J. E. Straub , D. Thirumalai

The self-assembly of proteins into $\beta$-sheet-rich amyloid fibrils has been observed to occur with sigmoidal kinetics, indicating that the system initially is trapped in a metastable state. Here, we use a minimal lattice-based model to…

Biological Physics · Physics 2016-01-05 Anders Irbäck , Jonas Wessén