Gold surfaces functionalized with nickel-nitrilotriacetic acid (Ni2+-NTA) as self-assembled monolayers (SAM) to immobilize histidine (His)-tagged biomolecules are broadly reported in the literature. However, the increasing demand of using microfluidic systems and biosensors takes more and more advantage on silicon technology which provides dedicated glass surfaces and substantially allows cost and resource savings. Here we present a novel method for the controlled oriented immobilization of His-tagged proteins on glass surfaces functionalized with a Ni2+-NTA layer. Exemplarily, the protein pattern morphology after immobilization on the Ni2+-NTA layer of His6-tagged soluble receptor for advanced glycation endproducts (sRAGE) was investigated and compared to non-oriented immobilization of sRAGE on amino SAM by using scanning electron microscopy (SEM). Moreover, we demonstrated interaction of immobilized sRAGE with three structurally different ligands, S100A12, S100A4, and glycated low density lipoproteins (glycLDL), by means of peak-force tapping atomic force microscopy (PF-AFM). We showed a clear discrimination of different protein-ligand orientations by differential height measurements.
AlexiouP., ChatzopoulouM., PegklidouK. and DemopoulosV.J., RAGE: A multi-ligand receptor unveiling novel insights in health and disease, Current Medicinal Chemistry17 (2010), 2232–2252.
2.
BaltusR.E., CarmonK.S. and LuckL.A., Quartz crystal microbalance (QCM) with immobilized protein receptors: Comparison of response to ligand binding for direct protein immobilization and protein attachment via disulfide linker, Langmuir23 (2007), 3880–3885.
3.
CherkoukC., RebohleL. and SkorupaW., Bioconjugation of the estrogen receptor hERα to a quantum dot dye for a controlled immobilization on a SiO2 surface, Journal of Colloid and Interface Science355 (2011), 442–447.
4.
FritzG., RAGE: A single receptor fits multiple ligands, Trends in Biochemical Sciences36 (2011), 625–632.
5.
GoodingJ.J. and DarwishN., The rise of self-assembled monolayers for fabricating electrochemical biosensors–an interfacial perspective, The Chemical Record12 (2012), 92–105.
6.
Haase-KohnC., WolfS., LenkJ. and PietzschJ., Copper-mediated cross-linking of S100A4, but not of S100A2, results in proinflammatory effects in melanoma cells, Biophysical and Biochemical Research Communications413 (2011), 494–498.
7.
HoppmannS., HaaseC., RichterS. and PietzschJ., Expression, purification and fluorine-18 radiolabeling of recombinant S100 proteins–potential probes for molecular imaging of receptor for advanced glycation endproducts (RAGE) in vivo, Protein Expression and Purification57 (2008), 143–152.
8.
HoppmannS., SteinbachJ. and PietzschJ., Scavenger receptors are associated with cellular interactions of S100A12 in vitro and in vivo, The International Journal of Biochemistry & Cell Biology42 (2010), 651–661.
9.
HouseR.P., PozzutoM., PatelP., DulyaninovaN.G., LiZ.H., ZencheckW.D., VitoloM.I., WeberD.J. and BresnickA.R., Two functional S100A4 monomers are necessary for regulating nonmuscle myosin-IIA and HCT116 cell invasion, Biochemistry50 (2011), 6920–6932.
10.
JungF., WischkeC. and LendleinA., Degradable, multifunctional cardiovascular implants: Challenges and hurdles, Materials Research Society Bulletin35 (2010), 607–613.
11.
JungF., BrauneS. and LendleinA., Haemocompatibility testing of biomaterials using human platelets, Clinical Hemorheology and Microcirculation53 (2013), 97–115.
12.
KangE., ParkJ.W., McClellanS.J., KimJ.M., HollandD.P., LeeG.U., FransesE.I., ParkK. and ThompsonD.H., Specific adsorption of histidine-tagged proteins on silica surfaces modified with Ni2+/NTA-derivatized poly(ethylene glycol), Langmuir23 (2007), 6281–6288.
13.
KimS.H., JeyakumarM. and KatzenellenbogenJ.A., Dual-mode fluorophore-doped nickel nitrilotriacetic acid-modified silica nanoparticles combine histidine-tagged protein purification with site-specific fluorophore labeling, Journal of the American Chemical Society129 (2007), 13254–13264.
14.
KohlerS., WeilbeerC., HowitzS., BeckerH., BeushausenV. and BelderD., PDMS free-flow electrophoresis chips with integrated partitioning bars for bubble segregation, Lab on a Chip11 (2011), 309–314.
15.
KoyamaH., YamamotoH. and NishizawaY., RAGE and soluble RAGE: Potential therapeutic targets for cardiovascular diseases, Molecular Medicine13 (2007), 625–635.
16.
LanatiN., EmanueleE., BrondinoN. and GeroldiD., Soluble RAGE-modulating drugs: State-of-the-art and future perspectives for targeting vascular inflammation, Current Vascular Pharmacology8 (2010), 86–92.
17.
LebeauL., LachF., Venien-BryanC., RenaultA., DietrichJ., JahnT., PalmgrenM.G., KühlbrandtW. and MioskowskiC., Two-dimensional crystallization of a membrane protein on a detergent-resistant lipid monolayer, Journal of Molecular Biology308 (2001), 639–647.
18.
MarlattN.M., BoysB.L., KonermannL. and ShawG.S., Formation of monomeric S100B and S100A11 proteins at low ionic strength, Biochemistry48 (2009), 1954–1963.
19.
MatinlinnaJ.P., ArevaS., LassilaL.V.J. and VallittuP.K., Characterization of siloxane films on titanium substrate derived from three aminosilanes, Surface and Interface Analysis36 (2004), 1314–1322.
20.
MauryP., EscalanteM., PeterM., ReinhoudtD.N., SubramaniamV. and HuskensJ., Creating nanopatterns of His-tagged proteins on surfaces by nanoimprint lithography using specific NiNTA-histidine interactions, Small3 (2007), 1584–1592.
21.
MorozO.V., DodsonG.G., WilsonK.S., LukanidinE. and BronsteinI.B., Multiple structural states of S100A12: A key to its functional diversity, Microscopy Research Technique60 (2003), 581–592.
22.
NoltingD.M., AzizE.F., OttossonN., FaubelM., HertelI.V. and WinterB., pH-induced protonation of lysine in aqueous solution causes chemical shifts in X-ray photoelectron spectroscopy, Journal of the American Chemical Society129 (2007), 14068–14073.
23.
OrlovaE.V., ShermanM.B., ChiuW., MowriH., SmithL.C. and GottoA.M.Jr., Three-dimensional structure of low density lipoproteins by electron cryomicroscopy, Proceedings of the National Academy of Sciences of the United States of America96 (1999), 8420–8425.
24.
PaborskyL.R., DunnK.E., GibbsC.S. and DoughertyJ.P., A nickel chelate microtiter plate assay for six histidine-containing proteins, Analytical Biochemistry234 (1996), 60–65.
25.
PaikH.J., KimY., OrthR.N., OberC.K, CoatesG.W. and BattC.A., (2005) End-functionalization of poly(3-hydroxybutyrate)via genetic engineering for solid surface modification, Chemical Communications (Cambridge)1956–1958.
26.
ParkH., AdsitF.G. and BoyingtonJ.C., The 1.5Å crystal structure of human receptor for advanced glycation endproducts (RAGE) ectodomains reveals unique features determining ligand binding, Journal of Biological Chemistry285 (2010), 40762–40770.
27.
PietzschJ., S100 proteins in health and disease, Amino Acids41 (2011), 755–760.
28.
PietzschJ. and HoppmannS., Human S100A12: A novel key player in inflammation?Amino Acids36 (2009), 381–389.
29.
PorathJ., CarlssonJ., OlssonI. and BelfrageG., Metal chelate affinity chromatography, a new approach to protein fractionation, Nature258 (1975), 598–599.
30.
ReynoldsN.P., TuckerJ.D., DavisonP.A., TimneyJ.A., HunterC.N. and LeggettG.J., J. Site-specific immobilization and micrometer and nanometer scale photopatterning of yellow fluorescent protein on glass surfaces, Journal of the American Chemical Society131 (2009), 896–897.
31.
SalazarR.B., ShovskyA., SchoenherrH. and VancsoG.J., Dip-pen nanolithography on (bio)reactive monolayer and block-copolymer platforms: Deposition of lines of single macromolecules, Small2 (2006), 1274–1282.
32.
SalzmanE.W., MerrillE.W. and KentK.C., Interaction of blood with artificial surfaces, In: ColmanR.W., HirshJ., MarderV.J. and SalzmanE.W. (eds.) Hemostasis and Thrombosis:Basic Principles and Clinical Practice. J.B. Lippincott Company, Philadelphia, USA, 1994, pp. 1469–1485.
33.
SamantaD. and SarkarA., Immobilization of bio-macromolecules on self-assembled monolayers: Methods and sensor applications, Chemical Society Reviews40 (2011), 2567–2592.
34.
Santamaria-KisielL., Rintala-DempseyA.C. and ShawG.S., Calcium-dependent and -independent interactions of the S100 protein family, Biochemical Journal396 (2006), 201–214.
35.
SárkányZ., IkonenT.P., Ferreira-da-SilvaF., SaraivaM.J., SvergunD. and DamasA.M., Solution structure of the soluble receptor for advanced glycation end products (sRAGE), Journal of Biological Chemistry286 (2011), 37525–37534.
36.
SavageB., SixmaJ.J. and RuggeriZ.M., Functional self-association of von Willebrand factor during platelet adhesion under flow, Proceedings of the National Academy of Sciences of the United States of America99 (2002), 425–430.
37.
SchmidtA.M., YanS.D., YanS.F. and SternD.M., The biology of the receptor for advanced glycation end products and its ligands, Biochimica Biophysica Acta1498 (2000), 99–111.
38.
SigalG.B., BamdadC., BarberisA., StromingerJ. and WhitesidesG.M., A self-assembled monolayer for the binding and study of histidine-tagged proteins by surface plasmon resonance, Analytical Chemistry68 (1996), 490–497.
39.
SivaramanB. and LatourR.A., Time-dependent conformational changes in adsorbed albumin and its effect on platelet adhesion, Langmuir28 (2012), 2745–2752.
40.
SmithR.K., LewisP.A. and WeissP.S., Patterning self-assembled monolayers, Progress in Surface Science75 (2004), 1–68.
41.
SoranH. and DurringtonP.N., Susceptibility of LDL and its subfractions to glycation, Current Opinion in Lipidology22 (2011), 254–261.
42.
TandlerN., MoschB. and PietzschJ., Protein and non-protein biomarkers in melanoma: A critical update, Amino Acids43 (2012), 2203–2230.
43.
TurchaninA., TinazliA., El-DesawyM., GrossmannH., SchnietzM., SolakH.H., TampeR. and GoelzhaeuserA., Molecular self-assembly, chemical lithography, and biochemical tweezers: A path for the fabrication of functional nanometer-scale protein arrays, Advanced Materials20 (2008), 471–477.
44.
WautierJ.L., andJ.L. and WautierM.P., Molecular basis of erythrocyte adhesion to endothelial cells in diseases, Clinical Hemorheology and Microcirculation53 (2013), 11–21.
45.
WolfS., Haase-KohnC., LenkJ., HoppmannS., BergmannR., SteinbachJ. and PietzschJ., Expression, purification and fluorine-18 radiolabeling of recombinant S100A4: A potential probe for molecular imaging of receptor for advanced glycation endproducts in vivo?Amino Acids41 (2011), 809–820.
46.
WuC.C., ReinhoudtD.N., OttoC., VeldersA.H. and SubramaniamV., Protein immobilization on Ni(II) ion patterns prepared by microcontact printing and dip-pen nanolithography, ACS Nano4 (2010), 1083–1091.
47.
ZimmermannR., PanzenböckU., WinterspergerA., Levak-FrankS., GraierW., GlatterO., FritzG., KostnerG.M. and ZechnerR., Lipoprotein lipase mediates the uptake of glycated LDL in fibroblasts, endothelial cells, and macrophages, Diabetes50 (2001), 1643–1653.
48.
ZhenG., FalconnetD., KuennemannE., VörösJ., SpencerN.D., TextorM. and ZürcherS., Nitrilotriacetic acid functionalized graft copolymers: A polymeric interface for selective and reversible binding of histidine-tagged proteins, Advanced Functional Materials16 (2006), 243–251.
