title: Accessing to the minor proteome of red blood cells through the influence of the nanoparticle surface properties on the corona composition.
abstract: Nanoparticle (NP)-protein interactions in complex samples have not yet been clearly understood. Nevertheless, several studies demonstrated that NP's physicochemical features significantly impact on the protein corona composition. Taking advantage of the NP potential to harvest different subsets of proteins, we assessed for the first time the capacity of three kinds of superparamagnetic NPs to highlight the erythrocyte minor proteome. Using both qualitative and quantitative proteomics approaches, nano-liquid chromatography-tandem mass spectrometry allowed the identification of 893 different proteins, confirming the reproducible capacity of NPs to increase the number of identified proteins, through a reduction of the sample concentration range and the capture of specific proteins on the three different surfaces. These NP-specific protein signatures revealed significant differences in their isoelectric point and molecular weight. Moreover, this NP strategy offered a deeper access to the erythrocyte proteome highlighting several signaling pathways implicated in important erythrocyte functions. The automated potentiality, the reproducibility, and the low-consuming sample demonstrate the strong compatibility of our strategy for large-scale clinical studies and may become a standardized sample preparation in future erythrocyte-associated proteomics studies.
authors.affiliation: Clinatec CEA-LETI, Grenoble, France.
authors.forename: Affif
authors.initials: A
authors.lastname: Zaccaria
authors.affiliation: CNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), Toulouse, France ; Université de Toulouse, UPS, IPBS, Toulouse, France.
authors.forename: Florence
authors.initials: F
authors.lastname: Roux-Dalvai
authors.affiliation: Clinatec CEA-LETI, Grenoble, France.
authors.forename: Ali
authors.initials: A
authors.lastname: Bouamrani
authors.affiliation: Clinatec CEA-LETI, Grenoble, France.
authors.forename: Adrien
authors.initials: A
authors.lastname: Mombrun
authors.affiliation: TIMC-THEREX UMR 5525 CNRS, UJF, CHU Grenoble, Grenoble, France.
authors.forename: Pascal
authors.initials: P
authors.lastname: Mossuz
authors.affiliation: CNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), Toulouse, France ; Université de Toulouse, UPS, IPBS, Toulouse, France.
authors.forename: Bernard
authors.initials: B
authors.lastname: Monsarrat
authors.affiliation: Clinatec CEA-LETI, Grenoble, France.
authors.forename: François
authors.initials: F
authors.lastname: Berger
mesh_terms: D000328:Adult; D001798:Blood Proteins / Q000032:analysis* / Q000378:metabolism; D002853:Chromatography, Liquid / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D004912:Erythrocytes / Q000737:chemistry / Q000378:metabolism*; D005260:Female; D006801:Humans; D058185:Magnetite Nanoparticles / Q000737:chemistry*; D008297:Male; D008875:Middle Aged; D020543:Proteome / Q000032:analysis / Q000378:metabolism; D040901:Proteomics / Q000379:methods; D015203:Reproducibility of Results; D013499:Surface Properties; D053719:Tandem Mass Spectrometry / Q000379:methods
chemical_list: D001798:Blood Proteins; D058185:Magnetite Nanoparticles; D020543:Proteome
keywords: mass spectrometry; minor proteome; nanoparticles; protein corona; quantitative proteomics; red blood cells
references.citation: Electrophoresis. 2001 Oct;22(16):3514-21
references.pmid: 11669535
references.citation: Proteomics. 2006 Mar;6(5):1399-414
references.pmid: 16447155
references.citation: Angew Chem Int Ed Engl. 2007;46(30):5754-6
references.pmid: 17591736
references.citation: ACS Nano. 2010 Jul 27;4(7):3623-32
references.pmid: 20553005
references.citation: Exp Biol Med (Maywood). 2007 Dec;232(11):1391-408
references.pmid: 18040063
references.citation: Trends Biotechnol. 2008 Aug;26(8):425-33
references.pmid: 18514941
references.citation: Biosens Bioelectron. 2010 Jul 15;25(11):2389-401
references.pmid: 20451366
references.citation: Mol Cell Proteomics. 2007 Sep;6(9):1621-37
references.pmid: 17533220
references.citation: ACS Nano. 2011 Sep 27;5(9):7503-9
references.pmid: 21861491
references.citation: PLoS One. 2010;5(6):e10949
references.pmid: 20532175
references.citation: Mol Cell Proteomics. 2010 May;9(5):1006-21
references.pmid: 20093276
references.citation: Neurosci Lett. 2009 Sep 29;463(1):6-11
references.pmid: 19631719
references.citation: Langmuir. 2004 Nov 23;20(24):10639-47
references.pmid: 15544396
references.citation: Science. 2003 Jan 10;299(5604):256-9
references.pmid: 12446870
references.citation: J Proteomics. 2011 Nov 18;74(12):2660-81
references.pmid: 21596164
references.citation: Proteomics. 2008 Feb;8(4):715-30
references.pmid: 18297650
references.citation: Trends Pharmacol Sci. 2010 May;31(5):199-205
references.pmid: 20172613
references.citation: Acc Chem Res. 2011 Oct 18;44(10):863-74
references.pmid: 21823593
references.citation: Mol Pharm. 2008 Jul-Aug;5(4):487-95
references.pmid: 18510338
references.citation: Lancet. 2000 Apr 8;355(9211):1260-8
references.pmid: 10770319
references.citation: Adv Drug Deliv Rev. 2009 Jun 21;61(6):428-37
references.pmid: 19376175
references.citation: Proc Natl Acad Sci U S A. 2008 Sep 23;105(38):14265-70
references.pmid: 18809927
references.citation: Mol Cell Proteomics. 2008 Nov;7(11):2254-69
references.pmid: 18614565
references.citation: ACS Nano. 2011 Sep 27;5(9):7155-67
references.pmid: 21866933
references.citation: Transfus Clin Biol. 2010 Sep;17(3):151-64
references.pmid: 20655788
references.citation: Nat Nanotechnol. 2012 Dec;7(12):779-86
references.pmid: 23212421
references.citation: Anal Chim Acta. 2012 Aug 31;740:58-65
references.pmid: 22840651
references.citation: Mol Cell Proteomics. 2006 Oct;5(10):1727-44
references.pmid: 16887931
references.citation: Lancet. 2000 Apr 1;355(9210):1169-75
references.pmid: 10791394
references.citation: BMC Proc. 2009 Jul 16;3 Suppl 4:S6
references.pmid: 19615119
references.citation: Nat Mater. 2009 Jul;8(7):543-57
references.pmid: 19525947
references.citation: Brief Funct Genomic Proteomic. 2008 Sep;7(5):329-39
references.pmid: 18579615
references.citation: Neurobiol Dis. 2012 Jun;46(3):607-24
references.pmid: 22426390
references.citation: Indian J Med Res. 2005 Feb;121(2):111-5
references.pmid: 15756044
references.citation: Anal Bioanal Chem. 2015 Jan;407(3):845-54
references.pmid: 25168116
references.citation: J Proteomics. 2012 Mar 16;75(6):1924-32
references.pmid: 22266103
references.citation: Nat Protoc. 2006;1(2):880-91
references.pmid: 17406321
references.citation: Proc Natl Acad Sci U S A. 1998 May 26;95(11):6469-73
references.pmid: 9600990
references.citation: Mol Cell Proteomics. 2002 Nov;1(11):845-67
references.pmid: 12488461
references.citation: Neurosci Lett. 2010 Aug 9;480(1):78-82
references.pmid: 20540987
references.citation: Blood. 2006 Jan 1;107(1):98-105
references.pmid: 16174757
references.citation: Nat Rev Cancer. 2005 Mar;5(3):161-71
references.pmid: 15738981
references.citation: Curr Opin Biotechnol. 2007 Dec;18(6):565-71
references.pmid: 18160274
references.citation: Blood. 2006 Dec 1;108(12):3637-45
references.pmid: 16882712
references.citation: Anal Chem. 2004 Mar 15;76(6):1560-70
references.pmid: 15018552
references.citation: Chem Rev. 2011 Sep 14;111(9):5610-37
references.pmid: 21688848
references.citation: J Proteome Res. 2008 Jul;7(7):3060-3
references.pmid: 18494517
references.citation: Curr Mol Med. 2010 Mar;10(2):133-41
references.pmid: 20196732
references.citation: AAPS J. 2010 Dec;12(4):504-18
references.pmid: 20549403
references.citation: Bioinformatics. 2006 Jun 15;22(12):1540-2
references.pmid: 16595560