Coaggregation of κ-Casein and β-Lactoglobulin Produces Morphologically Distinct Amyloid Fibrils

Small ◽  
2017 ◽  
Vol 13 (14) ◽  
pp. 1603591 ◽  
Author(s):  
Jared K. Raynes ◽  
Li Day ◽  
Pauline Crepin ◽  
Mathew H. Horrocks ◽  
John A. Carver
Keyword(s):  
Amyloid Fibrils ◽  
Β Lactoglobulin

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

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

scholarly journals Relaxation dynamics in bio-colloidal cholesteric liquid crystals confined to cylindrical geometry

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Sayyed Ahmad Khadem ◽  
Massimo Bagnani ◽  
Raffaele Mezzenga ◽  
Alejandro D. Rey
Keyword(s):  
Electric Fields ◽  
Cellulose Nanocrystals ◽  
Amyloid Fibrils ◽  
Underlying Mechanism ◽  
Stimuli Responsive ◽  
Relaxation Dynamics ◽  
Cholesteric Phase ◽  
Nematic Phases ◽  
Experimental Findings ◽  
Β Lactoglobulin

Abstract Para-nematic phases, induced by unwinding chiral helices, spontaneously relax to a chiral ground state through phase ordering dynamics that are of great interest and crucial for applications such as stimuli-responsive and biomimetic engineering. In this work, we characterize the cholesteric phase relaxation behaviors of β-lactoglobulin amyloid fibrils and cellulose nanocrystals confined into cylindrical capillaries, uncovering two different equilibration pathways. The integration of experimental measurements and theoretical predictions reveals the starkly distinct underlying mechanism behind the relaxation dynamics of β-lactoglobulin amyloid fibrils, characterized by slow equilibration achieved through consecutive sigmoidal-like steps, and of cellulose nanocrystals, characterized by fast equilibration obtained through smooth relaxation dynamics. Particularly, the specific relaxation behaviors are shown to emerge from the order parameter of the unwound cholesteric medium, which depends on chirality and elasticity. The experimental findings are supported by direct numerical simulations, allowing to establish hard-to-measure viscoelastic properties without applying magnetic or electric fields.

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

Magnetic-Responsive Hybrids of Fe3O4 Nanoparticles with β-Lactoglobulin Amyloid Fibrils and Nanoclusters

ACS Nano ◽  
2013 ◽  
Vol 7 (7) ◽  
pp. 6146-6155 ◽  
Author(s):  
Sreenath Bolisetty ◽  
Jijo J. Vallooran ◽  
Jozef Adamcik ◽  
Raffaele Mezzenga
Keyword(s):  
Fe3o4 Nanoparticles ◽  
Amyloid Fibrils ◽  
Β Lactoglobulin

scholarly journals Amyloid-Fibril Based Membranes for PFAS Removal from Water

2021 ◽  
Author(s):  
Tonghui Jin ◽  
Mohammad Peydayesh ◽  
Hanna Joerss ◽  
Jiangtao Zhou ◽  
Sreenath Bolisetty ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Efficient Approach ◽  
Polyfluoroalkyl Substances ◽  
Β Lactoglobulin ◽  
Adsorption Capability ◽  
Long Chain

We introduce a green and efficient approach for removing per- and polyfluoroalkyl substances (PFASs) based on the β-Lactoglobulin amyloid fibrils membrane. The membrane exhibits superior adsorption capability for long-chain PFASs....

Folic acid inhibits the amyloid fibrils formation of β-lactoglobulin

2017 ◽  
Vol 1 (1) ◽  
pp. 22 ◽  
Author(s):  
Baoliang Ma ◽  
Wen Li ◽  
Xudong Zhu ◽  
Guiling Liu ◽  
Fan Zhang ◽  
...  
Keyword(s):  
Folic Acid ◽  
Amyloid Fibrils ◽  
Β Lactoglobulin

Characterisation of amyloid fibrils formed from β-lactoglobulin

2002 ◽  
Vol 30 (3) ◽  
pp. A83-A83
Author(s):  
Walraj S. Gosal ◽  
Simon B. Ross-Murphy ◽  
Paul D. A. Pudney ◽  
Allan H. Clark
Keyword(s):  
Amyloid Fibrils ◽  
Β Lactoglobulin
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