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....

scholarly journals Polysaccharide-reinforced amyloid fibril hydrogels and aerogels

Nanoscale ◽  
2021 ◽  
Author(s):  
Mattia Usuelli ◽  
Till Germerdonk ◽  
Yiping Cao ◽  
Mohammad Peydayesh ◽  
Massimo Bagnani ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Drug Delivery ◽  
Cell Growth ◽  
Water Purification ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
High Interest ◽  
Β Lactoglobulin

β-Lactoglobulin amyloid fibrils are bio-colloids of high interest in many fields (e.g. water purification, cell growth, drug delivery and sensing). While the mechanical properties of pure amyloid fibril gels meet...

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.

scholarly journals The Ultrastructure of Tissue Damage by Amyloid Fibrils

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4611
Author(s):  
Haruki Koike ◽  
Masahisa Katsuno
Keyword(s):  
Tissue Damage ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Prion Diseases ◽  
Nerve Biopsy ◽  
Al Amyloidosis ◽  
Amyloid Fibril Formation ◽  
Autopsy Specimens ◽  
Fibril Aggregates ◽  
Interfering Rna

Amyloidosis is a group of diseases that includes Alzheimer’s disease, prion diseases, transthyretin (ATTR) amyloidosis, and immunoglobulin light chain (AL) amyloidosis. The mechanism of organ dysfunction resulting from amyloidosis has been a topic of debate. This review focuses on the ultrastructure of tissue damage resulting from amyloid deposition and therapeutic insights based on the pathophysiology of amyloidosis. Studies of nerve biopsy or cardiac autopsy specimens from patients with ATTR and AL amyloidoses show atrophy of cells near amyloid fibril aggregates. In addition to the stress or toxicity attributable to amyloid fibrils themselves, the toxicity of non-fibrillar states of amyloidogenic proteins, particularly oligomers, may also participate in the mechanisms of tissue damage. The obscuration of the basement and cytoplasmic membranes of cells near amyloid fibrils attributable to an affinity of components constituting these membranes to those of amyloid fibrils may also play an important role in tissue damage. Possible major therapeutic strategies based on pathophysiology of amyloidosis consist of the following: 1) reducing or preventing the production of causative proteins; 2) preventing the causative proteins from participating in the process of amyloid fibril formation; and/or 3) eliminating already-deposited amyloid fibrils. As the development of novel disease-modifying therapies such as short interfering RNA, antisense oligonucleotide, and monoclonal antibodies is remarkable, early diagnosis and appropriate selection of treatment is becoming more and more important for patients with amyloidosis.

Binding of long chain fatty acids to β-lactoglobulin

Lipids ◽  
1970 ◽  
Vol 5 (4) ◽  
pp. 403-411 ◽  
Author(s):  
Arthur A. Spector ◽  
John E. Fletcher
Keyword(s):  
Fatty Acids ◽  
Long Chain Fatty Acids ◽  
Β Lactoglobulin ◽  
Long Chain ◽  
Chain Fatty Acids

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

Inhibition of Amyloid Fibril Growth and Dissolution of Amyloid Fibrils by Curcumin-Gold Nanoparticles

2014 ◽  
Vol 20 (20) ◽  
pp. 6184-6191 ◽  
Author(s):  
Sharbari Palmal ◽  
Amit Ranjan Maity ◽  
Brijesh Kumar Singh ◽  
Sreetama Basu ◽  
Nihar R. Jana ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Amyloid Fibrils ◽  
Amyloid Fibril

scholarly journals Molecular dynamics simulations of mechanical failure in polymorphic arrangements of amyloid fibrils containing structural defects

2013 ◽  
Vol 4 ◽  
pp. 429-440 ◽  
Author(s):  
Hlengisizwe Ndlovu ◽  
Alison E Ashcroft ◽  
Sheena E Radford ◽  
Sarah A Harris
Keyword(s):  
Mechanical Properties ◽  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Steered Molecular Dynamics ◽  
Mechanical Failure ◽  
Structural Defects ◽  
Dynamics Simulations

We examine how the different steric packing arrangements found in amyloid fibril polymorphs can modulate their mechanical properties using steered molecular dynamics simulations. Our calculations demonstrate that for fibrils containing structural defects, their ability to resist force in a particular direction can be dominated by both the number and molecular details of the defects that are present. The simulations thereby suggest a hierarchy of factors that govern the mechanical resilience of fibrils, and illustrate the general principles that must be considered when quantifying the mechanical properties of amyloid fibres containing defects.

scholarly journals The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid

2021 ◽  
Vol 118 (3) ◽  
pp. e2014442118
Author(s):  
Nir Salinas ◽  
Einav Tayeb-Fligelman ◽  
Massimo D. Sammito ◽  
Daniel Bloch ◽  
Raz Jelinek ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Membrane Damage ◽  
Fibril Formation ◽  
Regulation Mechanism ◽  
Bacterial Cells ◽  
Amyloid Fibril Formation ◽  
Β Amyloid ◽  
Β Sheets

Antimicrobial activity is being increasingly linked to amyloid fibril formation, suggesting physiological roles for some human amyloids, which have historically been viewed as strictly pathological agents. This work reports on formation of functional cross-α amyloid fibrils of the amphibian antimicrobial peptide uperin 3.5 at atomic resolution, an architecture initially discovered in the bacterial PSMα3 cytotoxin. The fibrils of uperin 3.5 and PSMα3 comprised antiparallel and parallel helical sheets, respectively, recapitulating properties of β-sheets. Uperin 3.5 demonstrated chameleon properties of a secondary structure switch, forming mostly cross-β fibrils in the absence of lipids. Uperin 3.5 helical fibril formation was largely induced by, and formed on, bacterial cells or membrane mimetics, and led to membrane damage and cell death. These findings suggest a regulation mechanism, which includes storage of inactive peptides as well as environmentally induced activation of uperin 3.5, via chameleon cross-α/β amyloid fibrils.

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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