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Article

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Title

Towards understanding the binding affinity of lipid drug carriers to serum albumin

Authors

[ 1 ] Instytut Technologii i Inżynierii Chemicznej, Wydział Technologii Chemicznej, Politechnika Poznańska | [ 2 ] Instytut Fizyki, Wydział Inżynierii Materiałowej i Fizyki Technicznej, Politechnika Poznańska | [ P ] employee | [ D ] phd student

Scientific discipline (Law 2.0)

[2.8] Materials engineering
[7.6] Chemical sciences

Year of publication

2023

Published in

Chemistry and Physics of Lipids

Journal year: 2023 | Journal volume: vol. 250

Article type

scientific article

Publication language

english

Keywords
EN
  • lipid monolayer
  • lipid−protein interaction
  • serum albumin
  • drug binding
Abstract

EN In the past several years there has been a rapid rise in the use of lipid-based drug formulations. In the case of intravenous drug administration the interaction of lipid carrier with serum albumin is crucial for the distribution of the bioactive molecules in the bloodstream and reaching the target tissue. In this work, we have explored the interaction of serum albumin with three-component lipid monolayer build of palmitoyloleoylphosphatidylcholine (POPC), sphingomyelin (SM), and cholesterol (Chol). Using wide range of lipid compositions and various concentrations of serum albumin we identified the factors governing the lipid-protein binding. Our study revealed that albumin can penetrate selectively the monolayers of POPC/SM/Chol depending on the lipid composition in the mixture. Moreover, the interaction of albumin with monolayer can be controlled by the molecular density of the film and the concentration of protein. The adsorbed albumin exists in the film on the top of lipid monolayer. This behavior may lead to the increase of the size and charge of the lipid carrier and affect the drug transport throughout the bloodstream. The results of this work provide essential physicochemical data that can be used for predicting the pharmacokinetic profile of lipid-based formulations.

Date of online publication

09.12.2022

Pages (from - to)

105271-1 - 105271-12

DOI

10.1016/j.chemphyslip.2022.105271

URL

https://www.sciencedirect.com/science/article/pii/S0009308422000998?via%3Dihub

Comments

Article Number: 105271

License type

Czasopismo hybrydowe

Ministry points / journal

100

Impact Factor

3,4

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