Title
Binding of α-lactalbumin to unsaturated fatty acids monolayers at various pH
Authors
[ 1 ] Instytut Technologii i Inżynierii Chemicznej, Wydział Technologii Chemicznej, Politechnika Poznańska | [ P ] employee | [ D ] phd student
Scientific discipline (Law 2.0)
Year of publication
2026
Published in
Article type
scientific article
Publication language
english
Keywords
EN
- Fatty acid
- Whey protein
- α-lactalbumin
- Langmuir monolayer
- Liprotides
- Infant formula
- HAMLET complex
Abstract
EN Interactions between unsaturated fatty acids (UFAs) and α-lactalbumin (α-LA) at biological interfaces play a crucial role in the formation of liprotides, which are the lipid–protein complexes with reported antitumor and antimicrobial activity. Here, we investigate the interfacial behavior of monolayers formed by various C18 unsaturated fatty acids: elaidic acid (EA), linoleic acid (LA), linolenic acid (LnA), and cis-vaccenic acid (VA) in the absence and presence of α-LA at two physiologically relevant pH values (2.00 for the stomach and 6.25 for the mouth and duodenum). Our findings reveal that both fatty acid structure and subphase pH profoundly influence monolayer organization, protein incorporation, and film stability over time. The analysis of kinetic experiments and compression–expansion cycles shows that at pH 2.00, EA forms the most stable complexes with α-LA, resembling the behavior of previously studied oleic acid. In contrast, at pH 6.25, LnA and VA demonstrate a stronger ability to incorporate α-LA driven by hydrophobic forces between exposed nonpolar protein residues and fatty acid chains. These results emphasize the importance of protein conformation, particularly the molten globule state of α-LA at low pH, in modulating interfacial interactions. Our study demonstrates that selected unsaturated fatty acids can form stable interfacial complexes with α-lactalbumin, expanding the range of alternatives to oleic acid. It also highlights how monolayer composition and pH influence the physicochemical design of functional foods, infant formulas, and lipid-based delivery systems. The insights presented in this work provide a foundation for further exploration of the biological activity and therapeutic relevance of UFAs-protein assemblies beyond conventional models.
Date of online publication
30.10.2025
Pages (from - to)
112187-1 - 112187-11
Comments
Article number: 112187
License type
other
Ministry points / journal
140
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