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
Nanomaterials ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 146
Author(s):  
Rocío Jurado ◽  
Natividad Gálvez

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.


2012 ◽  
Vol 13 (10) ◽  
pp. 3241-3252 ◽  
Author(s):  
Sreenath Bolisetty ◽  
Ludger Harnau ◽  
Jin-mi Jung ◽  
Raffaele Mezzenga

2019 ◽  
Vol 123 (50) ◽  
pp. 10877-10889 ◽  
Author(s):  
Georgi G. Gochev ◽  
Ernesto Scoppola ◽  
Richard A. Campbell ◽  
Boris A. Noskov ◽  
Reinhard Miller ◽  
...  

Author(s):  
Mario Barteri ◽  
Maria Cristina Gaudiano ◽  
Simona Rotella ◽  
Giuseppe Benagiano ◽  
Alessandro Pala

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Sayyed Ahmad Khadem ◽  
Massimo Bagnani ◽  
Raffaele Mezzenga ◽  
Alejandro D. Rey

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.


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