Literature DB >> 23455715

The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions.

Raffaele Mezzenga1, Peter Fischer.   

Abstract

The aggregation of proteins is of fundamental relevance in a number of daily phenomena, as important and diverse as blood coagulation, medical diseases, or cooking an egg in the kitchen. Colloidal food systems, in particular, are examples that have great significance for protein aggregation, not only for their importance and implications, which touches on everyday life, but also because they allow the limits of the colloidal science analogy to be tested in a much broader window of conditions, such as pH, ionic strength, concentration and temperature. Thus, studying the aggregation and self-assembly of proteins in foods challenges our understanding of these complex systems from both the molecular and statistical physics perspectives. Last but not least, food offers a unique playground to study the aggregation of proteins in three, two and one dimensions, that is to say, in the bulk, at air/water and oil/water interfaces and in protein fibrillation phenomena. In this review we will tackle this very ambitious task in order to discuss the current understanding of protein aggregation in the framework of foods, which is possibly one of the broadest contexts, yet is of tremendous daily relevance.

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Year:  2013        PMID: 23455715     DOI: 10.1088/0034-4885/76/4/046601

Source DB:  PubMed          Journal:  Rep Prog Phys        ISSN: 0034-4885


  18 in total

1.  Sulfate anion delays the self-assembly of human insulin by modifying the aggregation pathway.

Authors:  Marta Owczarz; Paolo Arosio
Journal:  Biophys J       Date:  2014-07-01       Impact factor: 4.033

2.  Fucoidan improves the structural integrity and the molecular stability of β-lactoglobulin.

Authors:  Hyun-Woong Park; Do-Yeong Kim; Weon-Sun Shin
Journal:  Food Sci Biotechnol       Date:  2018-04-11       Impact factor: 2.391

Review 3.  Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.

Authors:  Gang Wei; Zhiqiang Su; Nicholas P Reynolds; Paolo Arosio; Ian W Hamley; Ehud Gazit; Raffaele Mezzenga
Journal:  Chem Soc Rev       Date:  2017-07-31       Impact factor: 54.564

4.  Gap-plasmon based broadband absorbers for enhanced hot-electron and photocurrent generation.

Authors:  Yuhua Lu; Wen Dong; Zhuo Chen; Anders Pors; Zhenlin Wang; Sergey I Bozhevolnyi
Journal:  Sci Rep       Date:  2016-07-29       Impact factor: 4.379

Review 5.  Measurement of amyloid formation by turbidity assay-seeing through the cloud.

Authors:  Ran Zhao; Masatomo So; Hendrik Maat; Nicholas J Ray; Fumio Arisaka; Yuji Goto; John A Carver; Damien Hall
Journal:  Biophys Rev       Date:  2016-11-23

6.  Controlled self-assembly of plant proteins into high-performance multifunctional nanostructured films.

Authors:  Ayaka Kamada; Marc Rodriguez-Garcia; Francesco Simone Ruggeri; Yi Shen; Aviad Levin; Tuomas P J Knowles
Journal:  Nat Commun       Date:  2021-06-10       Impact factor: 14.919

7.  Colloidal Stability & Conformational Changes in β-Lactoglobulin: Unfolding to Self-Assembly.

Authors:  Steven Blake; Samiul Amin; Wei Qi; Madhabi Majumdar; E Neil Lewis
Journal:  Int J Mol Sci       Date:  2015-08-03       Impact factor: 5.923

8.  In-situ quantification of the interfacial rheological response of bacterial biofilms to environmental stimuli.

Authors:  Patrick A Rühs; Lukas Böni; Gerald G Fuller; R Fredrik Inglis; Peter Fischer
Journal:  PLoS One       Date:  2013-11-11       Impact factor: 3.240

9.  The Influence of Arginine on the Response of Enamel Matrix Derivative (EMD) Proteins to Thermal Stress: Towards Improving the Stability of EMD-Based Products.

Authors:  Alessandra Apicella; Peggy Heunemann; Sreenath Bolisetty; Matteo Marascio; Anja Gemperli Graf; Laszlo Garamszegi; Raffaele Mezzenga; Peter Fischer; Christopher J Plummer; Jan-Anders Månson
Journal:  PLoS One       Date:  2015-12-15       Impact factor: 3.240

10.  Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform.

Authors:  Kadi-Liis Saar; Emma V Yates; Thomas Müller; Séverine Saunier; Christopher M Dobson; Tuomas P J Knowles
Journal:  Biophys J       Date:  2016-02-02       Impact factor: 4.033

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