Interactions of Whey Proteins with Metal Ions

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Abstract

Whey proteins tend to interact with metal ions, which have implications in different fields related to human life quality. There are two impacts of such interactions: they can provide opportunities for applications in food and nutraceuticals, but may lead to analytical challenges related to their study and outcomes for food processing, storage, and food interactions. Moreover, interactions of whey proteins with metal ions are complicated, requiring deep understanding, leading to consequences, such as metalloproteins, metallocomplexes, nanoparticles, or aggregates, creating a biologically active system. To understand the phenomena of metal–protein interactions, it is important to develop analytical approaches combined with studies of changes in the biological activity and to analyze the impact of such interactions on different fields. The aim of this review was to discuss chemistry of β-lactoglobulin, α-lactalbumin, and lactotransferrin, their interactions with different metal ions, analytical techniques used to study them and the implications for food and nutraceuticals.

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Most cited references 113

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Proteomic analysis of post-translational modifications.

Matthias Mann, Ole N. Jensen (2003)

Post-translational modifications modulate the activity of most eukaryote proteins. Analysis of these modifications presents formidable challenges but their determination generates indispensable insight into biological function. Strategies developed to characterize individual proteins are now systematically applied to protein populations. The combination of function- or structure-based purification of modified 'subproteomes', such as phosphorylated proteins or modified membrane proteins, with mass spectrometry is proving particularly successful. To map modification sites in molecular detail, novel mass spectrometric peptide sequencing and analysis technologies hold tremendous potential. Finally, stable isotope labeling strategies in combination with mass spectrometry have been applied successfully to study the dynamics of modifications.

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Lactoferrin a multiple bioactive protein: An overview ☆

Isui Abril García-Montoya, Tania Siqueiros Cendón, Sigifredo Arévalo-Gallegos … (2011)

Background Lactoferrin (Lf) is an 80 kDa iron-binding glycoprotein of the transferrin family. It is abundant in milk and in most biological fluids and is a cell-secreted molecule that bridges innate and adaptive immune function in mammals. Its protective effects range from anticancer, anti-inflammatory and immune modulator activities to antimicrobial activities against a large number of microorganisms. This wide range of activities is made possible by mechanisms of action involving not only the capacity of Lf to bind iron but also interactions of Lf with molecular and cellular components of both hosts and pathogens. Scope of review This review summarizes the activities of Lf, its regulation and potential applications. Major conclusions The extensive uses of Lf in the treatment of various infectious diseases in animals and humans has been the driving force in Lf research however, a lot of work is required to obtain a better understanding of its activity. General significance The large potential applications of Lf have led scientists to develop this nutraceutical protein for use in feed, food and pharmaceutical applications. This article is part of a Special Issue entitled Molecular Mechanisms of Iron Transport and Disorders.

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Lactoferrin: an important host defence against microbial and viral attack.

G. Antonini, P. Valenti (2005)

The first function attributed to lactoferrin (Lf), an iron binding protein belonging to the non-immune natural defences, was antimicrobial activity that depended on its capacity to sequester iron. Iron-independent microbicidal activities, requiring direct interaction between this cationic protein and microbial surface components, were later demonstrated. Many other anti-microbial and anti-viral functions have since been ascribed to Lf. In mucosal secretions, iron and Lf modulate the motility and aggregation of pathogenic bacteria. Lf inhibits bacterial adhesion on abiotic surfaces through ionic binding to biomaterials, or specific binding to bacterial structures or both. Lf inhibition of bacterial adhesion to host cells requires Lf binding to bacteria and/or host cells. Lf hinders microbial internalization by binding to both glycosaminoglycans and bacterial proteins which can be degraded by Lf-mediated proteolysis. Moreover, Lf internalisation and localisation to the host cell nuclei could modulate bacterial entry into cells through gene regulation. Finally, the capability of Lf to exert antiviral activity, through its binding to host cells and/or viral particles, strengthens the idea that it is an important brick in the mucosal wall, effective against both microbial and viral attacks.

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Author and article information

Journal

Journal ID (nlm-ta): Int J Mol Sci

Journal ID (iso-abbrev): Int J Mol Sci

Journal ID (publisher-id): ijms

Title: International Journal of Molecular Sciences

Publisher: MDPI

ISSN (Electronic): 1422-0067

Publication date (Electronic): 20 March 2020

Publication date Collection: March 2020

Volume: 21

Issue: 6

Electronic Location Identifier: 2156

Affiliations

[1 ]Department of Environmental Chemistry and Bioanalysis, Faculty of Chemistry, Nicolaus Copernicus University, Gagarina 7, 87-100 Toruń, Poland; agnieszka.rodzik1@ 123456gmail.com (A.R.); sagandykova.gulyaim1@ 123456gmail.com (G.N.S.); bbusz@ 123456chem.umk.pl (B.B.)

[2 ]Centre for Modern Interdisciplinary Technologies, Nicolaus Copernicus University, Wileńska 4, 87-100 Toruń, Poland

Author notes

[* ]Correspondence: p.pomastowski@ 123456umk.pl ; Tel.: +48-56-6114308; Fax: +48-56-6656038

Author information

Paweł Pomastowski https://orcid.org/0000-0002-1594-0623

Bogusław Buszewski https://orcid.org/0000-0002-5482-7500

Article

Publisher ID: ijms-21-02156

DOI: 10.3390/ijms21062156

PMC ID: 7139725

PubMed ID: 32245108

SO-VID: 45074262-266c-4b65-92a7-e07c8ddf569e

License:

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

Interactions of Whey Proteins with Metal Ions

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Abstract

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Most cited references 113

Proteomic analysis of post-translational modifications.

Lactoferrin a multiple bioactive protein: An overview ☆

Lactoferrin: an important host defence against microbial and viral attack.

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