Shotgun proteomic analytical approach for studying proteins adsorbed onto liposome surface

Type
Article

Authors
Capriotti, Anna Laura
Caracciolo, Giulio
Cavaliere, Chiara
Crescenzi, Carlo
Pozzi, Daniela
Laganà, Aldo

KAUST Grant Number
KUK-F1-036-32

Online Publication Date
2011-07-02

Print Publication Date
2011-09

Date
2011-07-02

Abstract
The knowledge about the interaction between plasma proteins and nanocarriers employed for in vivo delivery is fundamental to understand their biodistribution. Protein adsorption onto nanoparticle surface (protein corona) is strongly affected by vector surface characteristics. In general, the primary interaction is thought to be electrostatic, thus surface charge of carrier is supposed to play a central role in protein adsorption. Because protein corona composition can be critical in modifying the interactive surface that is recognized by cells, characterizing its formation onto lipid particles may serve as a fundamental predictive model for the in vivo efficiency of a lipidic vector. In the present work, protein coronas adsorbed onto three differently charged cationic liposome formulations were compared by a shotgun proteomic approach based on nano-liquid chromatography-high-resolution mass spectrometry. About 130 proteins were identified in each corona, with only small differences between the different cationic liposome formulations. However, this study could be useful for the future controlled design of colloidal drug carriers and possibly in the controlled creation of biocompatible surfaces of other devices that come into contact with proteins into body fluids. © 2011 Springer-Verlag.

Citation
Capriotti AL, Caracciolo G, Cavaliere C, Crescenzi C, Pozzi D, et al. (2011) Shotgun proteomic analytical approach for studying proteins adsorbed onto liposome surface. Analytical and Bioanalytical Chemistry 401: 1195–1202. Available: http://dx.doi.org/10.1007/s00216-011-5188-8.

Acknowledgements
This publication is based on work supported by Award No. KUK-F1-036-32, made by King Abdullah University of Science and Technology (KAUST).

Publisher
Springer Nature

Journal
Analytical and Bioanalytical Chemistry

DOI
10.1007/s00216-011-5188-8

PubMed ID
21725631

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