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Biophysical study of the effect of ovalbumin and lysozyme in DMPC/sphingomyelin/cholesterol bilayers

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Abstract

The cell is separated from the external environment by a lipid bilayer. In this biological interface, phospholipids and proteins play relevant roles on both the outer and inner sides. Understanding lipid–protein interactions is important to advance our knowledge of the relation between membrane properties and cell’s functions in order to reveal the driving forces behind membrane-related processes and to develop new biomedical applications. To this end, one strategy is to study lipid–protein interactions by determining thermodynamic properties of lipid membrane models in interactions with proteins. In this work, we present a systematic biophysical investigation exploring how changes in membrane properties promote the interaction of proteins with the lipid bilayer. We studied the interaction of ovalbumin (OVA) and lysozyme (LYZ) with DMPC/sphingomyelin/cholesterol (MSC) membranes (using large unilamellar vesicles, LUVs, as membrane models) by differential scanning calorimetry (DSC) and dynamic light scattering (DLS). Our results show that lipid bilayer composition, large incubation time periods, and the membrane phase are determinants to induce nonspecific lipid–protein interactions at the level of the lipid bilayer-water interface, significantly modifying the membrane thermal response. We demonstrated that cholesterol and sphingomyelin not only rule the thermodynamic properties of pure lipid membranes but also regulate the cooperativity and interactions in lipid/protein systems. Our results contribute to a better understanding of the driving forces of lipid–protein interactions in the bilayer and could be of practical reference for the designing and development of new applications related to biomembrane interactions, for example, smart drug delivery systems.

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Abbreviations

DSC:

Differential scanning calorimetry

DLS:

Dynamic light scattering

LUVs:

Large unilamellar vesicles

T m :

Phase transition temperature

C p :

Specific heat capacity at constant pressure

ΔH :

Enthalpy change

ΔT 1/2 :

The width of the transition at half peak height

DMPC:

1,2-Dimyristoyl-sn-glycero-3-phosphocholine

SM:

Sphingomyelin from brain porcine

Chol:

Cholesterol

OVA:

Albumin from chicken egg white

LYZ:

Lysozyme from chicken egg white

MSC:

1,2-Dimyristoyl-sn-glycero-3-phosphocholine/sphingomyelin/cholesterol

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Acknowledgements

RP-I thanks DGAPA-UNAM for a postdoctoral scholarship and acknowledges CONAHCYT-México for supporting in part the writing of this work via a postdoctoral fellowship. We thank Dra. Josefa Bernard for the use of her DLS equipment, Dra. Paola Moreno-Alvarez and Dr. Alfredo Cabrera-Orefice for their helpful comments on the manuscript.

Funding

This work was supported by DGAPA-UNAM Postdoctoral Grants Program, PAPIIT IN204616, and PAIP-FQ-UNAM 5000–9018.

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Authors and Affiliations

  1. Laboratorio de Bio-Fisicoquímica, Departamento de Fisicoquímica, Facultad de Química, Universidad Nacional Autónoma de México, 04510, Mexico City, Mexico

    R. Pérez-Isidoro, A. Jessica Díaz-Salazar & M. Costas

  2. Centro de Investigación en Química Aplicada (CIQA), Enrique Reyna, 140, 25294, Saltillo, Coahuila, Mexico

    R. Pérez-Isidoro

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  1. R. Pérez-Isidoro
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  3. M. Costas
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Contributions

Conceptualization: RP-I and MC; Methodology and data analysis: RP-I and AJD-S; Writing-original draft preparation: RP-I; Review and editing: RP-I, MC, and AJD-S; Funding acquisition: MC; Resources: RP-I, MC, and AJD-S; Supervision: RP-I and MC. All authors have read and agreed to the published version of the manuscript.

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Correspondence to R. Pérez-Isidoro or M. Costas.

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Pérez-Isidoro, R., Díaz-Salazar, A.J. & Costas, M. Biophysical study of the effect of ovalbumin and lysozyme in DMPC/sphingomyelin/cholesterol bilayers. J Therm Anal Calorim 149, 1219–1229 (2024). https://doi.org/10.1007/s10973-023-12784-z

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