4.7 Article

Amyloid-like aggregation influenced by lead(II) and cadmium(II) ions in hen egg white ovalbumin

Related references

Note: Only part of the references are listed.
Article Biochemistry & Molecular Biology

Protein stability [determination] problems

Faizan Ahmad

Summary: The correct folding of proteins is crucial for human health, but measuring or predicting protein stability under physiological conditions is challenging. Current measurement methods have limitations, including the need for extrapolation and the disregard for in vivo conditions.

FRONTIERS IN MOLECULAR BIOSCIENCES (2022)

Article Biochemistry & Molecular Biology

Effects of the Toxic Metals Arsenite and Cadmium on α-Synuclein Aggregation In Vitro and in Cells

Emma Lorentzon et al.

Summary: Exposure to arsenic and cadmium alters alpha-synuclein amyloid fiber structures and distribution within yeast cells, reducing aggregate clearance and aggravating toxicity. In vitro studies suggest interactions between these heavy metals and alpha-synuclein may modulate the pathogenesis of Parkinson's disease.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2021)

Article Chemistry, Multidisciplinary

Protein Nanofibrils and Their Hydrogel Formation with Metal Ions

Xinchen Ye et al.

Summary: Protein nanofibrils (PNFs) were prepared by whey protein fibrillation at low pH and in the presence of different metal ions. The metal ions' valence state and ionic radius significantly influenced the gelation behavior and fibrillation kinetics of the PNFs, with higher valence states and smaller ionic radii resulting in faster hydrogel formation. The presence of metal ions also affected the viscoelastic properties of the hydrogels, with more acidic metal ions inducing higher storage modulus compared to less acidic ones.

ACS NANO (2021)

Article Chemistry, Applied

Drying mode and hydrothermal treatment conditions govern the formation of amyloid-like protein fibrils in solutions of dried hen egg white

Margarita Monge-Morera et al.

Summary: It was found that dried hen egg white contains amyloid-like fibrils and the length of these fibrils can vary depending on drying and storage conditions. Research also determined optimal conditions for fibrillation of egg white proteins under different pH values, times, and temperatures. Additionally, it was observed that drying and storage conditions can impact the extent of protein fibrillation in dried egg white.

FOOD HYDROCOLLOIDS (2021)

Article Biochemistry & Molecular Biology

On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy

Jelica Milosevic et al.

Summary: The study investigates the use of FTIR spectroscopy for analyzing oligomeric intermediates on the pathway of amyloid fibrillation, showing the great potential of FTIR for qualitative and quantitative monitoring of oligomer formation based on the secondary structure changes.

MOLECULES (2021)

Article Spectroscopy

Exploring the potential of infrared spectroscopy in qualitative and quantitative monitoring of ovalbumin amyloid fibrillation

Jelica Milosevic et al.

SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY (2020)

Article Biochemistry & Molecular Biology

Processing Induced Changes in Food Proteins: Amyloid Formation during Boiling of Hen Egg White

Margarita Monge-Morera et al.

BIOMACROMOLECULES (2020)

Review Environmental Sciences

A Review on Heavy Metals Contamination in Soil: Effects, Sources, and Remediation Techniques

Changfeng Li et al.

SOIL & SEDIMENT CONTAMINATION (2019)

Article Chemistry, Applied

Assembly of iron-bound ovotransferrin amyloid fibrils

Zihao Wei et al.

FOOD HYDROCOLLOIDS (2019)

Review Food Science & Technology

Rational Design of Amyloid-Like Fibrillary Structures for Tailoring Food Protein Techno-Functionality and Their Potential Health Implications

Koen J. A. Jansens et al.

COMPREHENSIVE REVIEWS IN FOOD SCIENCE AND FOOD SAFETY (2019)

Review Chemistry, Multidisciplinary

Effects of in vivo conditions on amyloid aggregation

Michael C. Owen et al.

CHEMICAL SOCIETY REVIEWS (2019)

Article Chemistry, Multidisciplinary

On the role of peptide hydrolysis for fibrillation kinetics and amyloid fibril morphology

Xinchen Ye et al.

RSC ADVANCES (2018)

Article Multidisciplinary Sciences

Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation

Christine Xue et al.

ROYAL SOCIETY OPEN SCIENCE (2017)

Review Biochemistry & Molecular Biology

Functional Amyloids in Reproduction

Aveline Hewetson et al.

BIOMOLECULES (2017)

Review Biochemistry & Molecular Biology

ThT 101: a primer on the use of thioflavin T to investigate amyloid formation

Kirsten Gade Malmos et al.

AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS (2017)

Article Biochemistry & Molecular Biology

The Production of Curli Amyloid Fibers Is Deeply Integrated into the Biology of Escherichia coli

Daniel R. Smith et al.

BIOMOLECULES (2017)

Article Chemistry, Applied

Amyloid-like aggregation of ovalbumin: Effect of disulfide reduction and other egg white proteins

Koen J. A. Jansens et al.

FOOD HYDROCOLLOIDS (2016)

Article Environmental Sciences

Assessment of the bioaccumulation of metals to chicken eggs from residential backyards

Emily J. Grace et al.

SCIENCE OF THE TOTAL ENVIRONMENT (2016)

Article Biochemistry & Molecular Biology

Ferric Ions Inhibit the Amyloid Fibrillation of β-Lactoglobulin at High Temperature

Rita Guzzi et al.

BIOMACROMOLECULES (2015)

Article Biophysics

A Kinetic Study of Ovalbumin Fibril Formation: The Importance of Fragmentation and End-Joining

Jason M. D. Kalapothakis et al.

BIOPHYSICAL JOURNAL (2015)

Article Clinical Neurology

Amyloid deposition in Parkinson's disease and cognitive impairment: A systematic review

Myria Petrou et al.

MOVEMENT DISORDERS (2015)

Article Biochemistry & Molecular Biology

Metal ions modulate thermal aggregation of beta-lactoglobulin: A joint chemical and physical characterization

Giovanna Navarra et al.

JOURNAL OF INORGANIC BIOCHEMISTRY (2014)

Review Chemistry, Physical

Controlled food protein aggregation for new functionality

Taco Nicolai et al.

CURRENT OPINION IN COLLOID & INTERFACE SCIENCE (2013)

Article Biochemical Research Methods

Pattern prediction and coordination geometry analysis from cadmium-binding proteins: a computational approach

R. Jesu Jaya Sudan et al.

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2012)

Article Biochemistry & Molecular Biology

Self-Assembly of Ovalbumin into Amyloid and Non-Amyloid Fibrils

Cecile Lara et al.

BIOMACROMOLECULES (2012)

Article Chemistry, Applied

Encapsulation systems based on ovalbumin fibrils and high methoxyl pectin

K. N. P. Humblet-Hua et al.

FOOD HYDROCOLLOIDS (2011)

Article Chemistry, Applied

Food protein functionality: A comprehensive approach

E. Allen Foegeding et al.

FOOD HYDROCOLLOIDS (2011)

Article Biochemistry & Molecular Biology

The Mechanism of Fibril Formation of a Non-inhibitory Serpin Ovalbumin Revealed by the Identification of Amyloidogenic Core Regions

Naoki Tanaka et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2011)

Article Chemistry, Multidisciplinary

Influence of Protein Hydrolysis on the Growth Kinetics of β-Ig Fibrils

Ardy Kroes-Nijboer et al.

LANGMUIR (2011)

Review Pharmacology & Pharmacy

Protein aggregation-Pathways and influencing factors

Wei Wang et al.

INTERNATIONAL JOURNAL OF PHARMACEUTICS (2010)

Article Multidisciplinary Sciences

Identifying the amylome, proteins capable of forming amyloid-like fibrils

Lukasz Goldschmidt et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2010)

Article Biochemistry & Molecular Biology

A Comprehensive Model for Packing and Hydration for Amyloid Fibrils of β2-Microglobulin

Young-Ho Lee et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2009)

Article Biochemistry & Molecular Biology

Peptides are building blocks of heat-induced fibrillar protein aggregates of β-lactoglobulin formed at pH 2

Cynthia Akkermans et al.

BIOMACROMOLECULES (2008)

Article Chemistry, Multidisciplinary

Spectroscopic insights into lead(II) coordination by the selective lead(II)-binding protein PbrR691

Peng R. Chen et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2007)

Article Multidisciplinary Sciences

Atomic structures of amyloid cross-β spines reveal varied steric zippers

Michael R. Sawaya et al.

NATURE (2007)

Article Biochemistry & Molecular Biology

Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (Aβ) of Alzheimer's disease

CD Syme et al.

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS (2006)

Review Chemistry, Multidisciplinary

Reexamination of lead(II) coordination preferences in sulfur-rich sites: Implications for a critical mechanism of lead poisoning

JS Magyar et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2005)

Article Multidisciplinary Sciences

Structure of the cross-β spine of amyloid-like fibrils

R Nelson et al.

NATURE (2005)

Article Biophysics

Thermally induced fibrillar aggregation of hen egg white lysozyme

LN Arnaudov et al.

BIOPHYSICAL JOURNAL (2005)

Article Multidisciplinary Sciences

Sequence determinants of amyloid fibril formation

ML de la Paz et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2004)

Review Medicine, General & Internal

Molecular mechanisms of amyloidosis

G Merlini et al.

NEW ENGLAND JOURNAL OF MEDICINE (2003)

Article Chemistry, Physical

Network forming properties of various proteins adsorbed at the air/water interface in relation to foam stability

AH Martin et al.

JOURNAL OF COLLOID AND INTERFACE SCIENCE (2002)

Article Biochemical Research Methods

A holistic approach for protein secondary structure estimation from infrared spectra in H2O solutions

G Vedantham et al.

ANALYTICAL BIOCHEMISTRY (2000)

Article Biochemistry & Molecular Biology

Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain

MRH Krebs et al.

JOURNAL OF MOLECULAR BIOLOGY (2000)

Article Nutrition & Dietetics

Alzheimer's disease, β-amyloid protein and zinc

XD Huang et al.

JOURNAL OF NUTRITION (2000)

Article Biochemistry & Molecular Biology

α-to-β structural transformation of ovalbumin:: Heat and pH effects

HY Hu et al.

JOURNAL OF PROTEIN CHEMISTRY (2000)

Review Biochemistry & Molecular Biology

Amyloid fibrillogenesis: themes and variations

JC Rochet et al.

CURRENT OPINION IN STRUCTURAL BIOLOGY (2000)

Article Neurosciences

Amyloid-like inclusions in Huntington's disease

DP McGowan et al.

NEUROSCIENCE (2000)