Zemlyanov, Dmitry

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Purdue UniversityPurdue e-PubsBirck Poster Sessions Birck Nanotechnology Center4-2-2007XPS application for biologically related objectsDmitry ZemlyanovBirck Nanotechnology Center, Purdue University, dimazemlyanov@purdue.eduFollow this and additional works at: http://docs.lib.purdue.edu/nanoposterThis document has been made available through Purdue e-Pubs, a service of the Purdue University Libraries. Please contact epubs@purdue.edu foradditional information.Zemlyanov, Dmitry, "XPS application for biologically related objects" (2007). Birck Poster Sessions. Paper 12.http://docs.lib.purdue.edu/nanoposter/12Dmitry Zemlyanov, Birck Nanotechnology Center, Purdue University  Bich-Van Pham, Steve Beaudoin and Jaehyun Hur, You-Yeon Won, Department of Chemical Engineering, Purdue UniversitySabrina Jedlicka, Jenna Rickus, Department of Biological & Agricultural Engineering; Bindley Bioscience Center Purdue UniversitySOOOOH7AuSOOOOH7SOOOOH7SOOOOH7SOOOOH7In ideal PEG self-assembled monolayer: θ = 1 MLOrganic thin films, especially self-assembled monolayers (SAMs), are commonly used to modify surfaces in order reduce immunogenic responses and make implantable materials more biocompatible.  Polyethylene glycol (PEG) is one molecule that has been widely studied and shown to be able to reduce non specific protein adhesion and thereby improve biocompatibility. • How PEG is able to reduce non specific protein adhesion• How to properly create a PEG SAM with the correct distribution and arrangement. The cleaned gold substrates were then immersed into 0.01 M thiolated polyethylene glycol (PEG) acid (HSC2H4(OC2H4)8COOH) in ethanol. 290 285θ = 60°θ = 75°θ = 45°θ = 30°θ = 0°ResidualhydrocarbonsC-OC-C  Intensity, a.u.Binding Energy, eVPEG featuresO=C-OHθ PhotoemissionSample166 164 162 160S non-bound to Auθ = 60°θ = 75°θ = 45°θ = 30°θ = 0°  Bindimg Energy, eVθ PhotoemissionSampleS bound to Au-10 0 10 20 30 40 50 60 70 8020304050607080  Relative contribution, %Angle S bound to Au S non-bound to AuXPS of powder peptidesSOOOOH7AuSHOOOO7OHSOOOOH7HS O OO7SOOOOH7SOOOOH7Based on oxygen: θ = 0.68 MLBased on carbon: θ = 0.78 MLBased on sulfur: θ = 0.56 MLXPS conclusions on PEG SAM • Residual hydrocarbon;• Non-ideal adsorption: not complete  monolayer and upside-down configuration.Co-adsorption of EG thiol and acidic thiolHS OHOHS CH2 COOH16290 285ATEG/AT 1:3EG/AT 1:1EGAT featuresC-CC-OC-C  Intensity, a.u.Binding Energy, eVPEG featuresO=C-OHEG/AT 3:1EGEG/AT 3:1EG/AT 1:1EG/AT 1:3ATSolution010029.5270.4861.4038.6055.4644.5478.8621.14AT %EG %165 160S non-bound to Auθ = 60°θ = 0°  Bindimg Energy, eVθ PhotoemissionSample S bound to AuAuOOHSOOOOHSOOOOHSOOOOHSOOOOHSOOEG thiol:Based on carbon: θ = 0.9 MLBased on sulfur: θ = 0.6 MLHeight: 23.6Å (18.5 atomic bonds)XPS conclusions on co-adsorbed EG and AT• EG thiol forms the bond with Au through sulfur• Coverage of EG layer is close to ideal• AT layer contains up-side down configuration: sulfur group does not attached to AuHS O O O OHHS CH2 OCH2CH211OH3The integration of differentiated neurons into engineered devices has a high potential in implant biomedicine and cell-based biosensor application. This requires that cells must adhere on inorganic or hybrid materials and carry out normal metabolism, proliferation and differentiation. Sol-gel derived materials produced under biologically benign conditions have recently demonstrated high ability as substrates for adherent mammalian cells. The RGD and YIGSR peptides were also used to promote cellular adhesion, a phenomenon ofcrucial importance in the case of substrates for tissue engineering.SiO OOHNONHOHOHNOHNONHOHOHNONHHNNHNH2OHNOHNOHOONHHOONOHNOHN OHOOHRGD silaneSiOOOHNHNOH2NOOHNOH OONHONH2ONHOHNOHOONOHNOH2NONHOHNOHNOOHNID silaneSiO OOHNO NHONHHNHN NH2ONHOHNOHOHNO NHOHNOHO NHHN NHNH2OHNONHO OHYIG silaneSiOOOHN OH NHNNHH2NOHNOHOO NHOHNONHOHOOHNOHNOHNNH2OHNOOHOHNOHNOOHRDI silane295 290 285 280C*-CC*-N C*-OAmideO=C*-OH Experimental data Curve-fitting results  Intensity, arb. unitsBinding Energy, eVPeptide constraintsResidual HydrocarbonsC*F2θ = 0°YIGNIDRGDAngle Resolved XPSThe C 1s spectrum obtained from the powder RGD peptide at 0! collection angle.295 290 285 280θC*-CC*-N & C*-OAmideOH-C*=OC*N3 Experimental data Curve-fitting result   Intensity, arb. unitsBinding Energy, eVPeptide constraintResidual HydrocarbonsC*F2PhotoemissionSampleθ = 0°The number of carbon atoms in the different position and expected BE range (free peptides/peptide-silanes)11921418YIG free peptide121871320RGD silane121271320RDI silane-313-1218NID silane289.0-289.5288.5-289.6287.4-288.4286.4-287285.5-286.5284.6-285Binding Energy expected, eVC*-N3Type 6O=C*-OH (carboxyl)Type 5O=C*-N (amide)Type 4C*-O Type 3C*-N Type 2C*-CType 1The C 1s spectra obtained from surface YIG, RGD, NID silanes.XPS of surface peptidesOxygen to carbon and nitrogen to carbon ratios measured by XPS and expected from the surface peptide silane structure.0.333 / 1.639"0.01150.292 / 0.238"0.03313.3.0"0.4 / 6.2"0.4YIG silane0.423 / 4.828"0.8390.308 / 0.322"0.007619.0"1.6 / 10.8"1.4RGD silane0.361 / 1.2290.262 / 0.27217.7 / 11.1RDI silane0.449 / 3.2060.286 / 0.23910.2 / 5.3NID silaneO/Cpeptide Ideal/XPSN/Cpeptide Ideal/XPSCtotal / Cpeptide at %Coverage and adlayer height estimations0.085.8YIG silane0.1719.5RGD silane0.1531.3RDI silane0.0911.0NID silaneCoverage, Molecules per Si atoms on the surfaceHeight, ÅXPS conclusions on Sol-Gels Modified with Covalently Bound Peptides:• XPS is a new reliable tool for the characterization of organic thing film• Peptides and proteins can be quantified; the film quality can be examined

XPS application for biologically related objects

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XPS application for biologically related objects

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