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XPS와 AFM에 의한 올리고펩타이드의 자기 집합화 단분자막 분석
Analysis of Oligopeptide Self-Assembled Monolayer Using XPS and AFM
동아대학교 화학공학과, 604-714 부산시 사하구 하단2동 840 1경희대학교 화학공학과, 449-701 용인시 기흥읍 서천리 1 2티슈엔지니어링 연구센터 산업기술융합연구소, 1-1-1 Higashi, Tsukuba 305-8562
Department of Chemical Engineering, Dong-A University, 840 Hadan 2-dong, Saha-gu, Busan 604-714, Korea 1Department of Chemical Engineering, Kyunghee University, 1 Seochun-ri, Kiheung-eup, Yongin 449-701, Korea 2Tissue Engineering Research Center, The National Institute of Advanced Industrial Science and Technology, 1-1-1 Higashi, Tsukuba 305-8562, Japan
smjang@mail.donga.ac.kr
HWAHAK KONGHAK, February 2003, 41(1), 15-19(5), NONE
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Abstract
금속 기판 위에 유기 박막을 형성하는 방법 중에서 티올기와 Au와의 결합을 이용한 자기집합화에 관한 연구가 활발히 진행되고 있다. 포르피린 유도체와 강하게 결합하는 티올기를 가지는 올리고펩타이드 PSP1과 PSP2를 합성하여 MOPS 완충용액에서 금표면에 자기집합화 단분자막(self-assembled monolayer, SAM)을 형성시켜 X-ray photoelectron spectroscopy(XPS)와 atomic force microscopy(AFM)을 이용하여 분석하였다. 그 결과 PSP2의 경우가 PSP1의 경우보다 Au 표면에서 SAM이 더욱 더 잘 형성되고 있음을 알 수 있었고 MOPS 완충용액에 존재하는 황 이온의 영향도 알 수 있었다. 이 결과는 구성단위로부터 이론적으로 계산한 SAM막의 steric energy 값의 차이에서 유추한 결론과 일치하였다.
Recently, the self-assembled monolayer(SAM) of thiols on noble metals has been studied intensively. Oligopeptides such as PSP1(Tyr-Ala-Gly-Tyr-Cys) and PSP2(His-Ala-Ser-Tyr-Ser-Cys) with thiol group, which interact strongly with a typical cationic porphyrin derivative, are synthesized. Peptides adsorption from the liquid phase on Au has been studied using X-ray photoelectron spectroscopy(XPS) and AFM image. XPS provides further evidence that the primary adsorbate species is bonded to Au through the sulfur atom. By the analysis of XPS spectra and AFM image, it is found that PSP2 is self-assembled better than PSP1 and the sulfur ion in MOPS buffer solution has an effect on the self-assembling performance. This result is coincident with the calculation result of steric energies of Au-Peptide bonded SAM structure.
Keywords
References
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Strong L, Whitesides GM, Langmuir, 4(3), 546 (1988)
Samant MG, Brown CA, Gordon JG, Langmuir, 7(3), 437 (1991)
Whitesides GM, Laibinis PE, Langmuir, 6(1), 87 (1990)
Lawrence DS, Jiang T, Levett M, Chem. Rev., 95(6), 2229 (1995)
Yamada R, Uosaki K, Denki Kagaku, 65(6), 440 (1997)
Whelan CM, Smyth MR, Barnes CJ, Langmuir, 15(1), 116 (1999)
Chiang S, Science, 272(5265), 1123 (1996)
Poirier GE, Pylant ED, Science, 272(5265), 1145 (1996)
Takamura T, Matsushita K, Shimoyama Y, Jpn. J. Appl. Phys., 35, 5831 (1996)
Castner DG, Hinds K, Grainger DW, Langmuir, 12(21), 5083 (1996)
Laibinis PE, Bain CD, Whitesides GM, J. Phys. Chem., 95, 7017 (1991)
Walczak MM, Alves CA, Lamp BD, Porter MD, J. Electroanal. Chem., 396(1-2), 103 (1995)
Jager B, Schurmann H, Muller HU, Himmel HJ, Neumann M, Grunze M, Woll C, Z. Phys. Chem., 202, 263 (1997)
Biebuyck HA, Bian CD, Whitesides GM, Langmuir, 10(6), 1825 (1994)
Atherton E, Gait MJ, Sheppard RC, Willarns BJ, Bioorg. Chem., 351 (1979)
Noh J, Hara M, Langmuir, 16(5), 2045 (2000)
Carron KT, Hurley LG, J. Phys. Chem.-US, 95(24), 9979 (1991)
