Disassembly and in vitro cell compatibility of α-lactalbumin particulates under physiologically relevant conditions

Mai Bay Stie; Dirk Fennema Galparsoro; Xin Zhou; Vito Foderà

doi:10.1016/j.ejps.2024.106962

Disassembly and in vitro cell compatibility of α-lactalbumin particulates under physiologically relevant conditions

Mai Bay Stie^*, Dirk Fennema Galparsoro, Xin Zhou, Vito Foderà^*

^*Corresponding author for this work

Drug Delivery and Biophysics of Biopharmaceuticals

Research output: Contribution to journal › Journal article › Research › peer-review

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Abstract

Protein self-assemblies in the form of ordered supramolecular structures such as particulates hold great potential as new biomaterials. However, research in this field is rarely conducted under physiologically relevant conditions but such studies are crucially needed to unravel the potential use of particulates and other amyloid structures in health sciences. In this study, particulates of α-lactalbumin (ALA) were prepared at different stages of maturation by thermal incubation. Disassembly of particulates in isotonic buffer, neutral pH and at 37 °C was investigated by simultaneously measuring Thioflavin T fluorescence intensity and light scattering. Freshly formed particulates quickly disassembled and displayed complete release of soluble ALA within 1 h. Mature particulates displayed slower disassembly kinetics with incomplete release of ALA within 1 h. The biocompatibility of particulates at different maturation stages to epithelial lung and fibroblast cells was assessed in vitro. Good cell compatibility was observed in the presence of the particulates and their released species. Our findings display protein particulates as biodegradable and highly tunable particles, promoting them as good candidates for drug delivery purposes.

Original language	English
Article number	106962
Journal	European Journal of Pharmaceutical Sciences
Volume	204
Number of pages	7
ISSN	0928-0987
DOIs	https://doi.org/10.1016/j.ejps.2024.106962
Publication status	Published - 2025

Bibliographical note

Funding Information:
MBS, DFG, XZ, and VF acknowledge VILLUM FONDEN for the Villum Young Investigator Grant \u201CProtein superstructure as Smart Biomaterials (ProSmart)\u201D 2018\u20132023 (project number: 19175), and Novo Nordisk Foundation (project number NNF20OC0065260 and NNF22OC0080141) for funding the project. DFG acknowledges University of Palermo (FFR \u2013 PROMETA) for financial support. VF and XZ acknowledge China Scholarship Council (201709110108). Kleopatra Kalouta is acknowledged for her valuable input in the interpretation of the results. The authors acknowledge Davisco Food International/Agropur Ingredients (EdenPrairie, MN, USA) for providing the \u03B1-lactalbumin powder.

Publisher Copyright:
© 2024 The Author(s)

Keywords

Amyloids
Disassembly
Particulates
Protein aggregation
Protein self-assembly
Α-lactalbumin

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Cite this

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title = "Disassembly and in vitro cell compatibility of α-lactalbumin particulates under physiologically relevant conditions",

abstract = "Protein self-assemblies in the form of ordered supramolecular structures such as particulates hold great potential as new biomaterials. However, research in this field is rarely conducted under physiologically relevant conditions but such studies are crucially needed to unravel the potential use of particulates and other amyloid structures in health sciences. In this study, particulates of α-lactalbumin (ALA) were prepared at different stages of maturation by thermal incubation. Disassembly of particulates in isotonic buffer, neutral pH and at 37 °C was investigated by simultaneously measuring Thioflavin T fluorescence intensity and light scattering. Freshly formed particulates quickly disassembled and displayed complete release of soluble ALA within 1 h. Mature particulates displayed slower disassembly kinetics with incomplete release of ALA within 1 h. The biocompatibility of particulates at different maturation stages to epithelial lung and fibroblast cells was assessed in vitro. Good cell compatibility was observed in the presence of the particulates and their released species. Our findings display protein particulates as biodegradable and highly tunable particles, promoting them as good candidates for drug delivery purposes.",

keywords = "Amyloids, Disassembly, Particulates, Protein aggregation, Protein self-assembly, Α-lactalbumin",

author = "Stie, {Mai Bay} and {Fennema Galparsoro}, Dirk and Xin Zhou and Vito Foder{\`a}",

note = "Funding Information: MBS, DFG, XZ, and VF acknowledge VILLUM FONDEN for the Villum Young Investigator Grant \u201CProtein superstructure as Smart Biomaterials (ProSmart)\u201D 2018\u20132023 (project number: 19175), and Novo Nordisk Foundation (project number NNF20OC0065260 and NNF22OC0080141) for funding the project. DFG acknowledges University of Palermo (FFR \u2013 PROMETA) for financial support. VF and XZ acknowledge China Scholarship Council (201709110108). Kleopatra Kalouta is acknowledged for her valuable input in the interpretation of the results. The authors acknowledge Davisco Food International/Agropur Ingredients (EdenPrairie, MN, USA) for providing the \u03B1-lactalbumin powder. Publisher Copyright: {\textcopyright} 2024 The Author(s)",

year = "2025",

doi = "10.1016/j.ejps.2024.106962",

language = "English",

volume = "204",

journal = "European Journal of Pharmaceutical Sciences",

issn = "0928-0987",

publisher = "Elsevier",

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TY - JOUR

T1 - Disassembly and in vitro cell compatibility of α-lactalbumin particulates under physiologically relevant conditions

AU - Stie, Mai Bay

AU - Fennema Galparsoro, Dirk

AU - Zhou, Xin

AU - Foderà, Vito

N1 - Funding Information: MBS, DFG, XZ, and VF acknowledge VILLUM FONDEN for the Villum Young Investigator Grant \u201CProtein superstructure as Smart Biomaterials (ProSmart)\u201D 2018\u20132023 (project number: 19175), and Novo Nordisk Foundation (project number NNF20OC0065260 and NNF22OC0080141) for funding the project. DFG acknowledges University of Palermo (FFR \u2013 PROMETA) for financial support. VF and XZ acknowledge China Scholarship Council (201709110108). Kleopatra Kalouta is acknowledged for her valuable input in the interpretation of the results. The authors acknowledge Davisco Food International/Agropur Ingredients (EdenPrairie, MN, USA) for providing the \u03B1-lactalbumin powder. Publisher Copyright: © 2024 The Author(s)

PY - 2025

Y1 - 2025

N2 - Protein self-assemblies in the form of ordered supramolecular structures such as particulates hold great potential as new biomaterials. However, research in this field is rarely conducted under physiologically relevant conditions but such studies are crucially needed to unravel the potential use of particulates and other amyloid structures in health sciences. In this study, particulates of α-lactalbumin (ALA) were prepared at different stages of maturation by thermal incubation. Disassembly of particulates in isotonic buffer, neutral pH and at 37 °C was investigated by simultaneously measuring Thioflavin T fluorescence intensity and light scattering. Freshly formed particulates quickly disassembled and displayed complete release of soluble ALA within 1 h. Mature particulates displayed slower disassembly kinetics with incomplete release of ALA within 1 h. The biocompatibility of particulates at different maturation stages to epithelial lung and fibroblast cells was assessed in vitro. Good cell compatibility was observed in the presence of the particulates and their released species. Our findings display protein particulates as biodegradable and highly tunable particles, promoting them as good candidates for drug delivery purposes.

AB - Protein self-assemblies in the form of ordered supramolecular structures such as particulates hold great potential as new biomaterials. However, research in this field is rarely conducted under physiologically relevant conditions but such studies are crucially needed to unravel the potential use of particulates and other amyloid structures in health sciences. In this study, particulates of α-lactalbumin (ALA) were prepared at different stages of maturation by thermal incubation. Disassembly of particulates in isotonic buffer, neutral pH and at 37 °C was investigated by simultaneously measuring Thioflavin T fluorescence intensity and light scattering. Freshly formed particulates quickly disassembled and displayed complete release of soluble ALA within 1 h. Mature particulates displayed slower disassembly kinetics with incomplete release of ALA within 1 h. The biocompatibility of particulates at different maturation stages to epithelial lung and fibroblast cells was assessed in vitro. Good cell compatibility was observed in the presence of the particulates and their released species. Our findings display protein particulates as biodegradable and highly tunable particles, promoting them as good candidates for drug delivery purposes.

KW - Amyloids

KW - Disassembly

KW - Particulates

KW - Protein aggregation

KW - Protein self-assembly

KW - Α-lactalbumin

U2 - 10.1016/j.ejps.2024.106962

DO - 10.1016/j.ejps.2024.106962

M3 - Journal article

C2 - 39550896

AN - SCOPUS:85209073551

VL - 204

JO - European Journal of Pharmaceutical Sciences

JF - European Journal of Pharmaceutical Sciences

SN - 0928-0987

M1 - 106962

ER -