Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy

The aim of this study was to investigate binding interactions between β-lactoglobulin (BLG) and two different mucins, bovine submaxillary mucins (BSM) and porcine gastric mucin (PGM), using intrinsic and extrinsic fluorescence spectroscopies. Intrinsic fluorescence spectra showed an enhanced decreas...

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Autores principales:	Hilal Yılmaz, Seunghwan Lee, Ioannis S. Chronakis
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	fluorescence β-lactoglobulin bovine submaxillary mucin porcine gastric mucin pH Organic chemistry QD241-441
Acceso en línea:	https://doaj.org/article/f454a5be06334fe7b9e4a877df77cde6
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spelling	oai:doaj.org-article:f454a5be06334fe7b9e4a877df77cde62021-11-25T18:27:19ZInteractions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy10.3390/molecules262267991420-3049https://doaj.org/article/f454a5be06334fe7b9e4a877df77cde62021-11-01T00:00:00Zhttps://www.mdpi.com/1420-3049/26/22/6799https://doaj.org/toc/1420-3049The aim of this study was to investigate binding interactions between β-lactoglobulin (BLG) and two different mucins, bovine submaxillary mucins (BSM) and porcine gastric mucin (PGM), using intrinsic and extrinsic fluorescence spectroscopies. Intrinsic fluorescence spectra showed an enhanced decrease of fluorescence intensity of BLG at all pH conditions when BLG was mixed with PGM rather than with BSM. We propose that, unlike BSM, the tertiary structure of PGM changes and the hydrophobic regions are exposed at pH 3 due to protonation of negatively charged residues. Results suggest that PGM also facilitated the structural unfolding of BLG and its binding with PGM by a hydrophobic interaction, especially at acidic pH, which was further supported by extrinsic fluorescence spectroscopy. Hydrophobic interaction is suggested as the dominant interaction mechanism between BLG and PGM at pH 3, whereas electrostatic interaction is the dominant one between BLG and BSM.Hilal YılmazSeunghwan LeeIoannis S. ChronakisMDPI AGarticlefluorescenceβ-lactoglobulinbovine submaxillary mucinporcine gastric mucinpHOrganic chemistryQD241-441ENMolecules, Vol 26, Iss 6799, p 6799 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	fluorescence β-lactoglobulin bovine submaxillary mucin porcine gastric mucin pH Organic chemistry QD241-441
spellingShingle	fluorescence β-lactoglobulin bovine submaxillary mucin porcine gastric mucin pH Organic chemistry QD241-441 Hilal Yılmaz Seunghwan Lee Ioannis S. Chronakis Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy
description	The aim of this study was to investigate binding interactions between β-lactoglobulin (BLG) and two different mucins, bovine submaxillary mucins (BSM) and porcine gastric mucin (PGM), using intrinsic and extrinsic fluorescence spectroscopies. Intrinsic fluorescence spectra showed an enhanced decrease of fluorescence intensity of BLG at all pH conditions when BLG was mixed with PGM rather than with BSM. We propose that, unlike BSM, the tertiary structure of PGM changes and the hydrophobic regions are exposed at pH 3 due to protonation of negatively charged residues. Results suggest that PGM also facilitated the structural unfolding of BLG and its binding with PGM by a hydrophobic interaction, especially at acidic pH, which was further supported by extrinsic fluorescence spectroscopy. Hydrophobic interaction is suggested as the dominant interaction mechanism between BLG and PGM at pH 3, whereas electrostatic interaction is the dominant one between BLG and BSM.
format	article
author	Hilal Yılmaz Seunghwan Lee Ioannis S. Chronakis
author_facet	Hilal Yılmaz Seunghwan Lee Ioannis S. Chronakis
author_sort	Hilal Yılmaz
title	Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy
title_short	Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy
title_full	Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy
title_fullStr	Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy
title_full_unstemmed	Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy
title_sort	interactions of β-lactoglobulin with bovine submaxillary mucin vs. porcine gastric mucin: the role of hydrophobic and hydrophilic residues as studied by fluorescence spectroscopy
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/f454a5be06334fe7b9e4a877df77cde6
work_keys_str_mv	AT hilalyılmaz interactionsofblactoglobulinwithbovinesubmaxillarymucinvsporcinegastricmucintheroleofhydrophobicandhydrophilicresiduesasstudiedbyfluorescencespectroscopy AT seunghwanlee interactionsofblactoglobulinwithbovinesubmaxillarymucinvsporcinegastricmucintheroleofhydrophobicandhydrophilicresiduesasstudiedbyfluorescencespectroscopy AT ioannisschronakis interactionsofblactoglobulinwithbovinesubmaxillarymucinvsporcinegastricmucintheroleofhydrophobicandhydrophilicresiduesasstudiedbyfluorescencespectroscopy
_version_	1718411171865821184

Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy

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