Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates.

Literature DB >> 15169952

The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates.

Gian Gaetano Tartaglia¹, Andrea Cavalli, Riccardo Pellarin, Amedeo Caflisch.

Abstract

The mechanisms by which peptides and proteins form ordered aggregates are not well understood. Here we focus on the physicochemical properties of amino acids that favor ordered aggregation and suggest a parameter-free model that is able to predict the change of aggregation rates over a large set of natural sequences. Furthermore, the results of the parameter-free model correlate well with the aggregation propensities of a set of peptides designed by computer simulations.

Entities: Disease

Mesh：

Substances：

Year: 2004 PMID： 15169952 PMCID： PMC2279921 DOI： 10.1110/ps.04663504

Source DB: PubMed Journal: Protein Sci ISSN： 0961-8368 Impact factor: 6.725

14 in total

1. Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backbone.

Authors: A G Street; S L Mayo
Journal: Proc Natl Acad Sci U S A Date: 1999-08-03 Impact factor: 11.205

Review 2. Amyloid fibrillogenesis: themes and variations.

Authors: J C Rochet; P T Lansbury
Journal: Curr Opin Struct Biol Date: 2000-02 Impact factor: 6.809

3. A possible role for pi-stacking in the self-assembly of amyloid fibrils.

Authors: Ehud Gazit
Journal: FASEB J Date: 2002-01 Impact factor: 5.191

4. Evaluation of a fast implicit solvent model for molecular dynamics simulations.

Authors: Philippe Ferrara; Joannis Apostolakis; Amedeo Caflisch
Journal: Proteins Date: 2002-01-01

5. The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35.

Authors: Jörg Gsponer; Urs Haberthür; Amedeo Caflisch
Journal: Proc Natl Acad Sci U S A Date: 2003-04-16 Impact factor: 11.205

6. Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis.

Authors: Angela D Williams; Erik Portelius; Indu Kheterpal; Jun-tao Guo; Kelsey D Cook; Ying Xu; Ronald Wetzel
Journal: J Mol Biol Date: 2004-01-16 Impact factor: 5.469

7. Chain length dependence of apomyoglobin folding: structural evolution from misfolded sheets to native helices.

Authors: Clement C Chow; Charles Chow; Vinodhkumar Raghunathan; Theodore J Huppert; Erin B Kimball; Silvia Cavagnero
Journal: Biochemistry Date: 2003-06-17 Impact factor: 3.162

8. Hydrophobicity regained.

Authors: P A Karplus
Journal: Protein Sci Date: 1997-06 Impact factor: 6.725

9. Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect.

Authors: G I Makhatadze; P L Privalov
Journal: J Mol Biol Date: 1990-05-20 Impact factor: 5.469

10. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases.

Authors: Fabrizio Chiti; Martino Calamai; Niccolo Taddei; Massimo Stefani; Giampietro Ramponi; Christopher M Dobson
Journal: Proc Natl Acad Sci U S A Date: 2002-10-08 Impact factor: 11.205

50 in total

1. Converting the highly amyloidogenic human calcitonin into a powerful fibril inhibitor by three-dimensional structure homology with a non-amyloidogenic analogue.

Authors: Giuseppina Andreotti; Rosa Maria Vitale; Carmit Avidan-Shpalter; Pietro Amodeo; Ehud Gazit; Andrea Motta
Journal: J Biol Chem Date: 2010-11-15 Impact factor: 5.157

The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates.

1. Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backbone.

Review 2. Amyloid fibrillogenesis: themes and variations.

3. A possible role for pi-stacking in the self-assembly of amyloid fibrils.

4. Evaluation of a fast implicit solvent model for molecular dynamics simulations.

5. The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35.

6. Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis.

7. Chain length dependence of apomyoglobin folding: structural evolution from misfolded sheets to native helices.

8. Hydrophobicity regained.

9. Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect.

10. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases.

1. Converting the highly amyloidogenic human calcitonin into a powerful fibril inhibitor by three-dimensional structure homology with a non-amyloidogenic analogue.

2. Mutagenic exploration of the cross-seeding and fibrillation propensity of Alzheimer's beta-amyloid peptide variants.

3. Protein aggregation determinants from a simplified model: cooperative folders resist aggregation.

4. Organism complexity anti-correlates with proteomic beta-aggregation propensity.

5. Thermodynamic analysis of the aggregation propensity of oxidized Alzheimer's beta-amyloid variants.

6. Rational design of aggregation-resistant bioactive peptides: reengineering human calcitonin.

7. Mutagenic analysis of the nucleation propensity of oxidized Alzheimer's beta-amyloid peptide.

8. Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase.

9. Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptides.

10. The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution.