ArticlePLoS computational biology2009
Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine.
Article in PLoS computational biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Article
- Solvent induced amyloid polymorphism and the uncovering of the elusive class 3 amyloid topology.Communications biology · 2024Article
- Lung endothelium, tau, and amyloids in health and disease.Physiological reviews · 2024Review
- Heterogeneous and Allosteric Role of Surface Hydration for Protein-Ligand Binding.Journal of chemical theory and computation · 2023Article
- Simulations of cross-amyloid aggregation of amyloid-β and islet amyloid polypeptide fragments.Biophysical journal · 2022Article
- Impact of Electronic Polarization on Preformed, β-Strand Rich Homogenous and Heterogenous Amyloid Oligomers.Journal of computational biophysics and chemistry · 2022Article
- A New Function for Amyloid-Like Interactions: Cross-Beta Aggregates of Adhesins form Cell-to-Cell Bonds.Pathogens (Basel, Switzerland) · 2021Review
- MELD-accelerated molecular dynamics help determine amyloid fibril structures.Communications biology · 2021Article
- A theoretical study of polymorphism in VQIVYK fibrils.Biophysical journal · 2021Article
- Identification and characterization of the Hfq bacterial amyloid region DNA interactions.BBA advances · 2021Article
- Computational Investigation of Gantenerumab and Crenezumab Recognition of Aβ Fibrils in Alzheimer's Disease Brain Tissue.ACS chemical neuroscience · 2020Article
- Amyloid and the origin of life: self-replicating catalytic amyloids as prebiotic informational and protometabolic entities.Cellular and molecular life sciences : CMLS · 2018Article
- Effect of single point mutations in a form of systemic amyloidosis.Protein science : a publication of the Protein Society · 2015Article
- Probing the role of aromatic residues in the self-assembly of Aβ(16-22) in fluorinated alcohols and their aqueous mixtures.Biochemistry and biophysics reports · 2015Article
- Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Chemical reviews · 2015Review
- Structural Conversion of Aβ17-42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic Pathways.PLoS computational biology · 2015Article
- Stability of Iowa mutant and wild type Aβ-peptide aggregates.The Journal of chemical physics · 2014Article
- Article
- A kinetic approach to the sequence-aggregation relationship in disease-related protein assembly.The journal of physical chemistry. B · 2014Article
- Role of sequence and structural polymorphism on the mechanical properties of amyloid fibrils.PloS one · 2014Article
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
At the core of amyloid fibrils is the cross-beta spine, a long tape of beta-sheets formed by the constituent proteins. Recent high-resolution x-ray studies show that the unit of this filamentous structure is a beta-sheet bilayer with side chains within the bilayer forming a tightly interdigitating "steric zipper" interface. However, for a given peptide, different bilayer patterns are possible, and no quantitative explanation exists regarding which pattern is selected or under what condition there can be more than one pattern observed, exhibiting molecular polymorphism. We address the structural selection mechanism by performing molecular dynamics simulations to calculate the free energy of incorporating a peptide monomer into a beta-sheet bilayer. We test filaments formed by several types of peptides including GNNQQNY, NNQQ, VEALYL, KLVFFAE and STVIIE, and find that the patterns with the lowest binding free energy correspond to available atomistic structures with high accuracy. Molecular polymorphism, as exhibited by NNQQ, is likely because there are more than one most stable structures whose binding free energies differ by less than the thermal energy. Detailed analysis of individual energy terms reveals that these short peptides are not strained nor do they lose much conformational entropy upon incorporating into a beta-sheet bilayer. The selection of a bilayer pattern is determined mainly by the van der Waals and hydrophobic forces as a quantitative measure of shape complementarity among side chains between the beta-sheets. The requirement for self-complementary steric zipper formation supports that amyloid fibrils form more easily among similar or same sequences, and it also makes parallel beta-sheets generally preferred over anti-parallel ones. But the presence of charged side chains appears to kinetically drive anti-parallel beta-sheets to form at early stages of assembly, after which the bilayer formation is likely driven by energetics.
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