Elasticity in Physically Cross-Linked Amyloid Fibril Networks

被引:56
作者
Cao, Yiping [1 ]
Bolisetty, Sreenath [1 ]
Adamcik, Jozef [1 ]
Mezzenga, Raffaele [1 ,2 ]
机构
[1] ETH, Dept Hlth Sci & Technol, Schmelzbergstr 9, CH-8092 Zurich, Switzerland
[2] ETH, Dept Mat, Wolfgang Pauli Str 10, CH-8093 Zurich, Switzerland
关键词
BETA-LACTOGLOBULIN; ACTIN SOLUTIONS; DYNAMICS; GELATION; MECHANICS; RHEOLOGY; BEHAVIOR;
D O I
10.1103/PhysRevLett.120.158103
中图分类号
O4 [物理学];
学科分类号
070305 [高分子化学与物理];
摘要
We provide a constitutive model of semiflexible and rigid amyloid fibril networks by combining the affine thermal model of network elasticity with the Derjaguin-Landau-Vervey-Overbeek (DLVO) theory of electrostatically charged colloids. When compared to rheological experiments on beta-lactoglobulin and lysozyme amyloid networks, this approach provides the correct scaling of elasticity versus both concentration (G similar to c(2.2) and G similar to c(2.5) for semiflexible and rigid fibrils, respectively) and ionic strength (G similar to I-4.4 and G similar to I-3.8 for beta-lactoglobulin and lysozyme, independent from fibril flexibility). The pivotal role played by the screening salt is to reduce the electrostatic barrier among amyloid fibrils, converting labile physical entanglements into long-lived cross-links. This gives a power-law behavior of G with I having exponents significantly larger than in other semiflexible polymer networks (e.g., actin) and carrying DLVO traits specific to the individual amyloid fibrils.
引用
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页数:6
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