Simplified Exactly Solvable Model for β-Amyloid Aggregation

被引：15

作者：

Zamparo, M. ^{[1
]}

Trovato, A. ^{[1
]}

Maritan, A. ^{[1
,2
]}

机构：

[1] Univ Padua, Dipartimento Fis G Galilei, PD-35131 Padua, Italy

[2] Ist Nazl Fis Nucl, Sez Padova, PD-35131 Padua, Italy

来源：

PHYSICAL REVIEW LETTERS | 2010年 / 105卷 / 10期

关键词：

STATISTICAL MECHANICAL THEORY; PROTEIN CONFORMATION; KINETICS;

D O I：

10.1103/PhysRevLett.105.108102

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

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 well as a nontrivial dependence on the microscopic degrees of freedom of the single peptide chain, both in the alpha-helix folded isolated state and in the fibrillar one. The phase diagram of the model is studied and compared to the outcome of fibril formation experiments which is qualitatively reproduced.

引用

页数：4

共 25 条

[1] Analyses of simulations of three-dimensional lattice proteins in comparison with a simplified statistical mechanical model of protein folding [J].

Abe, H. ;

Wako, H. .

PHYSICAL REVIEW E, 2006, 74 (01)

[2] Exact solution of the Munoz-Eaton model for protein folding [J].

Bruscolini, P ;

Pelizzola, A .

PHYSICAL REVIEW LETTERS, 2002, 88 (25) :4

[3] Rate determining factors in protein model structures [J].

Bruscolini, Pierpaolo ;

Pelizzola, Alessandro ;

Zamparo, Marco .

PHYSICAL REVIEW LETTERS, 2007, 99 (03)

[4] Mutational analysis of the propensity for amyloid formation by a globular protein [J].

Chiti, F ;

Taddei, N ;

Bucciantini, M ;

White, P ;

Ramponi, G ;

Dobson, CM .

EMBO JOURNAL, 2000, 19 (07) :1441-1449

[5] Protein misfolding, functional amyloid, and human disease [J].

Chiti, Fabrizio ;

Dobson, Christopher M. .

ANNUAL REVIEW OF BIOCHEMISTRY, 2006, 75 :333-366

[6] Amyloid formation by globular proteins under native conditions [J].

Chiti, Fabrizio ;

Dobson, Christopher M. .

NATURE CHEMICAL BIOLOGY, 2009, 5 (01) :15-22

[7] The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation [J].

Fändrich, M ;

Dobson, CM .

EMBO JOURNAL, 2002, 21 (21) :5682-5690

[8] General structural motifs of amyloid protofilaments [J].

Ferguson, Neil ;

Becker, Johanna ;

Tidow, Henning ;

Tremmel, Sandra ;

Sharpe, Timothy D. ;

Krause, Gerd ;

Flinders, Jeremy ;

Petrovich, Miriana ;

Berriman, John ;

Oschkinat, Hartmut ;

Fersht, Alan R. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (44) :16248-16253

[9] Aggregation phenomena in a system of molecules with two internal states [J].

Gaspari, R. ;

Gliozzi, A. ;

Ferrando, R. .

PHYSICAL REVIEW E, 2007, 76 (04)

[10] RESPECTIVE ROLES OF SHORT-RANGE AND LONG-RANGE INTERACTIONS IN PROTEIN FOLDING [J].

GO, N ;

TAKETOMI, H .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1978, 75 (02) :559-563

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