Interactions of β-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy.
bovine submaxillary mucin
fluorescence
pH
porcine gastric mucin
β-lactoglobulin
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
10 Nov 2021
10 Nov 2021
Historique:
received:
20
10
2021
revised:
02
11
2021
accepted:
08
11
2021
entrez:
27
11
2021
pubmed:
28
11
2021
medline:
15
12
2021
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 34833889
pii: molecules26226799
doi: 10.3390/molecules26226799
pmc: PMC8623809
pii:
doi:
Substances chimiques
BSM1 protein, Bos taurus
0
Gastric Mucins
0
Lactoglobulins
0
Mucins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Bartin University
ID : 2019-FEN-A-015
Organisme : European Research Council
ID : 261152
Pays : International
Organisme : Innovationsfonden
ID : 7076-00053 B
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