Preferences help
enabled [disable] Abstract
Number of results
2014 | 12 | 5 | 568-576
Article title

TOF-SIMS surface analysis of L-Tryptophan self assembled monolayer

Title variants
Languages of publication
This paper dealt with the preparation and characterization of self - assembled monolayersSAM-s of 1-hexadecanethiole and mercapto acetic acid on the silver nanostructure and subsequently the immobilization with amino acid L-Tryptophane. In order to achieve it, we used the electrodeposition of silver onto nanostructured surface of paraffin impregnated graphite electrode (PIGE). Subsequently, we assembled SAM by choosing the 1-hexadecanethiole and mercaptoacetic acid. These two kinds of SAM underwent the functionalization by L-Tryptophan. The observations of silver on PIGE surfaces were performed by scanning electron microscope (SEM). For surface analysis of the SAM functionalized by L-tryphophan, the TOF-SIMS technique was chosen. Finally, the fragmented ions of the immobilized-L-Tryptophan SAM were determined on the basis of suggested residues and three-dimensional structure. The residues show that the ability of L-Tryptophan to build homogeneous structure is better by mercaptoacetic acid SAM structure than by 1-hexadecanethiol. It was observed that L-Tryptophan built compact surface, which, due its chemical properties, can represent very interesting side regarding biocompatibility, homochirality and robustness in the area of life science.
Physical description
1 - 5 - 2014
21 - 2 - 2014
  • University of Pavol Jozef Safarik, Trieda SNP1
  • University of Pavol Jozef Safarik, Trieda SNP1
  • University of Pavol Jozer Safarik
  • University of Pavol Jozer Safarik
  • [1] D.G. Castner, B.D. Ratner, Surf. Sci. 500, 28 (2002)[Crossref]
  • [2] C.A. Keller, K. Glasmästar, V.P. Zhdanov, B. Kasemo, Phys. Rev. Lett. 84, 5443 (2000)[Crossref]
  • [3] I. Pfeiffer, M. Zäch, Cellular and Subcellular Nanotechnology 113 (2013)
  • [4] M. Reches, E. Gazit, Current Nanoscience 2, 105 (2006)[Crossref]
  • [5] C.D. Bain, J. Evall, G.M. Whitesides, J. Am. Chem. Soc. 111, 7155 (1989)[Crossref]
  • [6] S.D. Evans, R. Sharma, A. Ulman, Langmuir 7, 156 (1991)[Crossref]
  • [7] A. Ulman, S.D. Evans, Y. Shnidman, R. Sharma, J.E. Eilers, J.C. Chang, Am. Chem. Soc. 113, 1499 (1991)[Crossref]
  • [8] P.E. Laibinis, R.G. Nuzzo, G.M. Whitesides, J. Phys. Chem. 96, 5097 (1992)[Crossref]
  • [9] P. Cuatrecasas, I. Parikh, Biochemistry 11, 2291 (1972)[Crossref]
  • [10] M.Y. Arica, H. Yavuz, S. Patir, A. Denizli, J. Mol. Catal. B: Enzym. 11, 127 (2000)[Crossref]
  • [11] Y. Xiao, H.-X. Ju, H.-Y. Chen, Anal. Chim. Acta 391, 73 (1999)[Crossref]
  • [12] A.T. Jagendorf, A. Patchornik, M. Sela, Biochim. Biophys. Acta 78, 516 (1963)[Crossref]
  • [13] R.F. Taylor, Anal. Chim. Acta 172, 241 (1985)[Crossref]
  • [14] W. Aehle, Enzymes in Industry, 2nd edition (Wiley, Weinheim, 2004)
  • [15] N. Vasileva, T. Godjevargova, Mater. Sci. Eng. C 25, 17 (2005)[Crossref]
  • [16] R. L. Willett, K. W. Baldwin, K. W. West, L. N. Pfeiffer, PNAS 102, 7817 (2005)[Crossref]
  • [17] M. Matsunaga, T. Nakanishi, T. Asahi, T. Osaka, Electrochem. Comm. 9, 725 (2007)[Crossref]
  • [18] N. Banno, T. Nakanishi, M. Matsunaga, T. Asahi, T. Osaka, J. Am. Chem. Soc. 126, 428 (2004)[Crossref]
  • [19] O. Hofstetter, H. Hofstetter, M. Wilchek, V. Schurig, B.S. Green, Nat. Biotechnol. 17, 371 (1999)[Crossref]
  • [20] Ch. Ruan, X. Chen, Y. Fang, J. Deng, Bioelectrochem. Bioenerg. 45, 287 (1998)[Crossref]
  • [21] I. Feliciano-Ramos, M. Caban-Acevedo, M.A. Scibioh, C.R. Cabrera, J. Electroanal. Chem. 650, 98 (2010)[Crossref]
  • [22] T.G. Lee, J. Kim, H.K. Shon, D. Jung, D.W. Moon, Appl. Surf. Sci. 252, 6632 (2006)[Crossref]
Document Type
Publication order reference
YADDA identifier
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.