High resolution synchrotron XPS study of L-cysteine and S-benzyl-L-cysteine on platinum: adhesion mechanisms and radiation damage

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dc.contributor.authorWong, Len_AU
dc.contributor.authorYayebjee, Men_AU
dc.contributor.authorStampfl, APJen_AU
dc.contributor.authorChen, CHen_AU
dc.contributor.authorWang, SCen_AU
dc.contributor.authorHuang, MLen_AU
dc.contributor.authorKlauser, Ren_AU
dc.date.accessioned2022-08-29T03:59:38Zen_AU
dc.date.available2022-08-29T03:59:38Zen_AU
dc.date.issued2006-12-07en_AU
dc.date.statistics2021-08-31en_AU
dc.description.abstractKey to the development of functional biomaterials and innovative technologies behind medical implants and biosensors is a deep understanding of the interaction between inorganic surfaces and biological systems at the molecular level. Amino acids adhered onto inorganic substrates are model systems which may be analysed at a fundamental level using x-ray photoelectron spectroscopy (XPS) [1]. L-cysteine has been proposed as a potential anchor for larger molecules, e.g. proteins, to adhere onto metals such as Au, due to cysteine’s reactive thiol group [2]. This paper presents a related but unexplored system: in-situ prepared L-cysteine on Pt{111}. Pt{111} is an atomically flat surface and is a relevant material, used in biosensors and medical implants. To compare the adhesion characteristics of small and large molecules, S-benzyl-L-cysteine on Pt{111} is also analysed. Core level binding energies are examined using high resolution XPS at the National Synchrotron Radiation Research Centre (NSRRC) in Taiwan. Analysis of S 2p binding energies indicates cysteine adsorption via the thiol group. Two N 1s peaks in the spectra suggest that cysteine is present in both neutral and zwitterionic forms. Analysis of S-Benzyl-L-Cysteine core level shifts demonstrates similar adhesion characteristics. An important consideration in the application of biosurfaces is the impact of x-ray irradiation. XPS, using an excitation energy of 480eV, is used to examine the damage to each surface, due to exposure from the x-ray beam. The dramatic evolution of the N 1s spectra from both molecules suggests cleavage of the amine group. In addition, C 1s spectra from L-cysteine and S-benzyl-L-cysteine show cleavage of the carboxyl group due to prolonged irradiation. [1] B. Kasemo, Surf. Sci., 500, 2002, 656. [2] O.Cavalleri, L. Oliveri, A. Daccà, R. Parodi and R. Rolandi, App. Surf. Sci., 175, 2001, 357en_AU
dc.identifier.citationWong, L., Tayebjee, M., Yu, D.-H., Stampfl, A., Chen, C.-H., Wang, S.-C., Huang, M.-L., & Klauser, R., (2006). High resolution synchrotron XPS study of L-cysteine and S-benzyl-L-cysteine on platinum: adhesion mechanisms and radiation damage. Paper presented at the Australian Instute of Physics 17th National Congress 2006, Brisbane Convention and Exhibition Centre, Brisbane Australia, Sunday 3 - Friday 8 December 2006. Retrieved from: https://www.aip.org.au/resources/Documents/Congress/AIPCongress-2006-Program.pdfen_AU
dc.identifier.conferenceenddate8 December 2006en_AU
dc.identifier.conferencenameAustralian Instute of Physics 17th National Congress 2006en_AU
dc.identifier.conferenceplaceBrisbane, Australiaen_AU
dc.identifier.conferencestartdate3 December 2006en_AU
dc.identifier.urihttps://www.aip.org.au/resources/Documents/Congress/AIPCongress-2006-Program.pdfen_AU
dc.identifier.urihttps://apo.ansto.gov.au/dspace/handle/10238/13646en_AU
dc.language.isoenen_AU
dc.publisherAustralian Institute of Physicsen_AU
dc.subjectSynchrotronsen_AU
dc.subjectX-ray photoelectron spectroscopyen_AU
dc.subjectCysteineen_AU
dc.subjectBenzyl alcoholen_AU
dc.subjectPlatinumen_AU
dc.subjectAdhesionen_AU
dc.subjectIrradiationen_AU
dc.subjectAmino acidsen_AU
dc.titleHigh resolution synchrotron XPS study of L-cysteine and S-benzyl-L-cysteine on platinum: adhesion mechanisms and radiation damageen_AU
dc.typeConference Abstracten_AU
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