Ms for Investigation of Time-Dependent Protein Adsorption On Surfaces in Complex Biological Samples

References

• Anderson JM , RodriguezA, ChangDT. Foreign body reaction to biomaterials. Semin. Immunol.20(2), 86–100 (2008).
   PubMed Web of Science ®Google Scholar
• Wisniewski N , KlitzmanB, MillerB, ReichertWM. Decreased analyte transport through implanted membranes: differentiation of biofouling from tissue effects. J. Biomed. Mater. Res.57(4), 513–521 (2001).
   Web of Science ®Google Scholar
• Sides CR , StenkenJA. Microdialysis sampling techniques applied to studies of the foreign body reaction. Eur. J. Pharm. Sci.57(), 74–86 (2014).
   PubMed Web of Science ®Google Scholar
• Rabe M , VerdesD, SeegerS. Understanding protein adsorption phenomena at solid surfaces. Adv. Colloid Interface Sci.162(1–2), 87–106 (2011).
   PubMed Web of Science ®Google Scholar
• Vroman L , AdamsA L, KlingsM, FischerG. Fibrinogen, globulins, albumin and plasma at interfaces. In: Applied Chemistry at Protein Interfaces. American Chemical Society, 255–289 (1975).
   Google Scholar
• Krishnan A , SturgeonJ, SiedleckiCA, VoglerEA. Scaled interfacial activity of proteins at the liquid–vapor interface. J. Biomed. Mater. Res. A68A(3), 544–557 (2004).
   Web of Science ®Google Scholar
• Cha P , KrishnanA, FioreVF, VoglerEA. Interfacial energetics of protein adsorption from aqueous buffer to surfaces with varying hydrophilicity. Langmuir24(6), 2553–2563 (2008).
   Web of Science ®Google Scholar
• Noh H , YoheST, VoglerEA. Volumetric interpretation of protein adsorption: ion-exchange adsorbent capacity, protein pi, and interaction energetics. Biomaterials29(13), 2033–2048 (2008).
   Web of Science ®Google Scholar
• Wei Q , BechererT, Angioletti-UbertiSet al. Protein interactions with polymer coatings and biomaterials. Angew. Chem. Int. Ed. Engl.53(31), 8004–8031 (2014).
   PubMed Web of Science ®Google Scholar
• Wagner MS , CastnerDG. Characterization of adsorbed protein films by time-of-flight secondary ion mass spectrometry with principal component analysis. Langmuir17(15), 4649–4660 (2001).
   Web of Science ®Google Scholar
• Wagner MS , HorbettTA, CastnerDG. Characterizing multicomponent adsorbed protein films using electron spectroscopy for chemical analysis, time-of-flight secondary ion mass spectrometry, and radiolabeling: capabilities and limitations. Biomaterials24(11), 1897–1908 (2003).
   Web of Science ®Google Scholar
• Mares J , ThongboonkerdV, TumaZ, MoravecJ, MatejovicM. Specific adsorption of some complement activation proteins to polysulfone dialysis membranes during hemodialysis. Kidney Int.76(4), 404–413 (2009).
   Web of Science ®Google Scholar
• Mares J , ThongboonkerdV, TumaZ, MoravecJ, KarvunidisT, MatejovicM. Proteomic analysis of proteins bound to adsorption units of extracorporeal liver support system under clinical conditions. J. Proteome Res.8(4), 1756–1764 (2009).
   Web of Science ®Google Scholar
• Wetterhall M , BergquistJ, HilleredL, HjortK, DahlinAP. Identification of human cerebrospinal fluid proteins and their distribution in an in vitro microdialysis sampling system. Eur. J. Pharm. Sci.57(), 34–40 (2014).
   Web of Science ®Google Scholar
• Dahlin A , HjortK, HilleredL, SjödinMD, BergquistJ, WetterhallM. Multiplexed quantification of proteins adsorbed to surface-modified and non-modified microdialysis membranes. Anal. Bioanal. Chem.402(6), 2057–2067 (2012).
   Web of Science ®Google Scholar
• Wetterhall M , ZuberovicA, HanriederJ, BergquistJ. Assessment of the partitioning capacity of high abundant proteins in human cerebrospinal fluid using affinity and immunoaffinity subtraction spin columns. J. Chromatogr. B878(19), 1519–1530 (2010).
   Web of Science ®Google Scholar
• Aebersold RH , LeavittJ, SaavedraRA, HoodLE, KentSB. Internal amino acid sequence analysis of proteins separated by one- or two-dimensional gel electrophoresis after in situ protease digestion on nitrocellulose. Proc. Natl Acad. Sci. USA84(20), 6970–6974 (1987).
   Web of Science ®Google Scholar
• Groseclose MR , AnderssonM, HardestyWM, CaprioliRM. Identification of proteins directly from tissue: in situ tryptic digestions coupled with imaging mass spectrometry. J. Mass Spectrom.42(2), 254–262 (2007).
   PubMed Web of Science ®Google Scholar
• Aguilar M-I , ClaytonDJ, HoltPet al. RP-HPLC binding domains of proteins. Anal. Chem.70(23), 5010–5018 (1998).
   Web of Science ®Google Scholar
• Ahmad-Tajudin A , AdlerB, EkströmSet al. Maldi-target integrated platform for affinity-captured protein digestion. Anal. Chim. Acta807(), 1–8 (2014).
   Web of Science ®Google Scholar
• Eng JK , MccormackAL, YatesIiiJR. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom.5(11), 976–989 (1994).
   PubMed Web of Science ®Google Scholar
• Thompson EJ . Proteins of the Cerebrospinal Fluid. Analysis & Interpretation in the Diagnosis and Treatment of Neurological Disease. Elsevier, London, UK (2005).
   Google Scholar
• Roche S , GabelleA, LehmannS. Clinical proteomics of the cerebrospinal fluid: towards the discovery of new biomarkers. Proteom. Clin. Appl.2(3), 428–436 (2008).
   Web of Science ®Google Scholar
• Fonslow BR , CarvalhoPC, AcademiaKet al. Improvements in proteomic metrics of low abundance proteins through proteome equalization using proteominer prior to mudpit. J. Proteome Res.10(8), 3690–3700 (2011).
   PubMed Web of Science ®Google Scholar
• Hirsh SL , MckenzieDR, NosworthyNJ, DenmanJA, SezermanOU, BilekMMM. The Vroman effect: competitive protein exchange with dynamic multilayer protein aggregates. Coll. Surf. B Biointerfaces103(), 395–404 (2013).
   Web of Science ®Google Scholar
• Vroman L , AdamsAL. Findings with the recording ellipsometer suggesting rapid exchange of specific plasma proteins at liquid/solid interfaces. Surf. Sci.16(), 438–446 (1969).
   Web of Science ®Google Scholar
• Liu H , SadygovRG, YatesJR. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem.76(14), 4193–4201 (2004).
   PubMed Web of Science ®Google Scholar
• Chelius D , BondarenkoPV. Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry. J. Proteome Res.1(4), 317–323 (2002).
   PubMed Web of Science ®Google Scholar
• Fairchild JN , WalworthMJ, HorváthK, GuiochonG. Correlation between peak capacity and protein sequence coverage in proteomics analysis by liquid chromatography-mass spectrometry/mass spectrometry. J. Chromatogr. A1217(29), 4779–4783 (2010).
   Web of Science ®Google Scholar
• Bantscheff M , SchirleM, SweetmanG, RickJ, KusterB. Quantitative mass spectrometry in proteomics: a critical review. Anal. Bioanal. Chem.389(4), 1017–1031 (2007).
   PubMed Web of Science ®Google Scholar
• Bantscheff M , LemeerS, SavitskiM, KusterB. Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present. Anal. Bioanal. Chem.404(4), 939–965 (2012).
   PubMed Web of Science ®Google Scholar
• Johnson RS , DavisMT, TaylorJA, PattersonSD. Informatics for protein identification by mass spectrometry. Methods35(3), 223–236 (2005).
   PubMed Web of Science ®Google Scholar
• Fonslow BR , SteinBD, WebbKJet al. Digestion and depletion of abundant proteins improves proteomic coverage. Nat. Meth.10(1), 54–56 (2013).
   Web of Science ®Google Scholar
• Ye M , PanY, ChengK, ZouH. Protein digestion priority is independent of protein abundances. Nat. Meth.11(3), 220–222 (2014).
   Web of Science ®Google Scholar