Shear-induced structure and mechanics of β-lactoglobulin amyloid fibrils

Soft Matter ◽  
2009 ◽  
Vol 5 (24) ◽  
pp. 5020 ◽  
Author(s):  
Dave E. Dunstan ◽  
Paul Hamilton-Brown ◽  
Peter Asimakis ◽  
William Ducker ◽  
Joseph Bertolini
Keyword(s):  
Amyloid Fibrils ◽  
Β Lactoglobulin ◽  
Shear Induced Structure ◽  
Induced Structure

scholarly journals Apoferritin Amyloid-Fibril Directed the In Situ Assembly and/or Synthesis of Optical and Magnetic Nanoparticles

Nanomaterials ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 146
Author(s):  
Rocío Jurado ◽  
Natividad Gálvez
Keyword(s):  
Metal Binding ◽  
Amyloid Fibrils ◽  
Magnetic Iron Oxide Nanoparticles ◽  
Synthetic Strategy ◽  
In Vivo Detection ◽  
Inorganic Species ◽  
Gold Silver ◽  
Β Lactoglobulin

The coupling of proteins that can assemble, recognise or mineralise specific inorganic species is a promising strategy for the synthesis of nanoscale materials with a controllable morphology and functionality. Herein, we report that apoferritin protein amyloid fibrils (APO) have the ability to assemble and/or synthesise various metal and metal compound nanoparticles (NPs). As such, we prepared metal NP–protein hybrid bioconjugates with improved optical and magnetic properties by coupling diverse gold (AuNPs) and magnetic iron oxide nanoparticles (MNPs) to apoferritin amyloid fibrils and compared them to the well-known β-lactoglobulin (BLG) protein. In a second approach, we used of solvent-exposed metal-binding residues in APO amyloid fibrils as nanoreactors for the in situ synthesis of gold, silver (AgNPs) and palladium nanoparticles (PdNPs). Our results demonstrate, the versatile nature of the APO biotemplate and its high potential for preparing functional hybrid bionanomaterials. Specifically, the use of apoferritin fibrils as vectors to integrate magnetic MNPs or AuNPs is a promising synthetic strategy for the preparation of specific contrast agents for early in vivo detection using various bioimaging techniques.

Foams Stabilized by β-Lactoglobulin Amyloid Fibrils: Effect of pH

2017 ◽  
Vol 65 (48) ◽  
pp. 10658-10665 ◽  
Author(s):  
Dengfeng Peng ◽  
Jinchu Yang ◽  
Jing Li ◽  
Cuie Tang ◽  
Bin Li
Keyword(s):  
Amyloid Fibrils ◽  
Effect Of Ph ◽  
Β Lactoglobulin

scholarly journals Rheological properties of hydroxypropylmethyl cellulose/sodium dodecylsulfate mixtures

2014 ◽  
Vol 79 (4) ◽  
pp. 457-468 ◽  
Author(s):  
Jaroslav Katona ◽  
Sandra Njaradi ◽  
Verica Sovilj ◽  
Lidija Petrovic ◽  
Brankica Marceta ◽  
...  
Keyword(s):  
Rheological Properties ◽  
Sodium Dodecylsulfate ◽  
Shear Thinning ◽  
Cellulose Ether ◽  
Flow Profile ◽  
Hydroxypropylmethyl Cellulose ◽  
Shear Rates ◽  
Newtonian Liquids ◽  
Shear Induced Structure ◽  
Induced Structure

Rheological properties of mixtures of hydroxypropylmethyl cellulose (HPMC), a nonionic associative cellulose ether, and sodium dodecylsulfate (SDS), an anionic surfactant, were investigated by viscosity measurements performed at different shear rates (0.1-6000 s-1). HPMC/SDS mixtures containing different concentrations of SDS (CSDS=0.00-3.50 % w/w) and HPMC concentrations which corresponded to the overlap parameter c/c*=3, 6, and 12 were prepared. All HPMC/SDS mixtures were found to be shear-thinning when examined in a low-end-to mid-range of the applied shear rates. The degree of shear-thinning, n, and viscosity of the mixtures were influenced by composition of HPMC/SDS mixtures and HPMC-SDS complex formation. The changes in n ranged from values typical for highly shear thinning to almost perfectly Newtonian liquids, and were more pronounced as c/c* was increased from 3 to 6 and 12. A change in flow profile and a buildup of the first normal stress difference (N1) was observed in HPMC/SDS mixtures with c/c*=6 and 12 and CSDS 0.55-1.00 % and 0.55-2.50 %, respectively, when a critical shear rate, crit. was exceeded, suggesting that a shear-induced structure formation in the mixtures took place.

Gelation, Phase Behavior, and Dynamics of β-Lactoglobulin Amyloid Fibrils at Varying Concentrations and Ionic Strengths

2012 ◽  
Vol 13 (10) ◽  
pp. 3241-3252 ◽  
Author(s):  
Sreenath Bolisetty ◽  
Ludger Harnau ◽  
Jin-mi Jung ◽  
Raffaele Mezzenga
Keyword(s):  
Phase Behavior ◽  
Amyloid Fibrils ◽  
Β Lactoglobulin
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