ICCAS OpenIR
Surface-enhanced Raman scattering studies on bombesin, its selected fragments and related peptides adsorbed at the silver colloidal surface
Podstawka-Proniewicz, Edyta1; Ozaki, Yukihiro2; Kim, Younkyoo3; Xu, Yizhuang4; Proniewicz, Leonard M.1,5
2011-07-15
Source PublicationAPPLIED SURFACE SCIENCE
ISSN0169-4332
Volume257Issue:19Pages:8246-8252
AbstractSERS studies presented in this work on BN8-14, [D-Phe(6), beta-Ala(11), Phe(13), Nle(14)]BN6-14, [D-Tyr(6), beta-Ala(11), Phe(13), Nle(14)]BN6-14, BN and its modified analogues, as well as NMB, NMC, and PG-L show that these molecules at pH 8.3 bind to a colloidal silver surface mainly through Trp(8) and Met(14) residues. Trp(8) adsorbs at the surface almost perpendicularly. Met(14) appears on the surface mainly as a PC-G conformer. His(12), as is evident from the spectra, practically does not take part in the adsorption process. Substitution of l-leucine at the 13 position of amino acid sequence with l-phenylalanine does not change substantially the pattern of the adsorption mechanism; however, substitution of phenylalanine at the 12 position (instead of l-histidine) causes changes in the SERS spectra that show that Phe(12) takes parallel orientation to the surface upon adsorption of [D-Phe(12)]BN, while in the case of [Tyr(4), D-Phe(12)]BN this residue is perpendicular to the surface and influences the orientation of the bound Trp(8). On the other hand, substitution of Asn with Tyr in the 6 position in nonapeptide fragment causes changes in the adsorption mechanism. In this case, the discussed fragment binds to the silver colloidal surface by Tyr(6), Trp(8), and Met(14). The SERS spectrum of NMC is very similar to that of BN; although it differs by the binding orientation of the amide bond towards the surface. Appearance of Phe(13) in NMB and PG-L causes that this residue competes successfully with Trp(8) forcing it to take tilted orientation. As seen from the enhancement of the characteristic Phe vibrations this moiety in NMB and PG-L adsorbs on the silver surface in a tilted fashion. This arrangements cause that the 8-14 peptide chain in all these studied compounds takes almost a parallel orientation to the surface while the 1-5 fragment of the peptide chain is removed from the silver surface vicinity. (C) 2011 Elsevier B. V. All rights reserved.
KeywordSurface-enhanced Raman Scattering Sers Colloidal Silver Surface Bombesin Bn Bn-related Peptides
DOI10.1016/j.apsusc.2011.02.012
Indexed BySCI ; ISTP
Language英语
WOS IDWOS:000291478000017
PublisherELSEVIER SCIENCE BV
Citation statistics
Cited Times:8[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.iccas.ac.cn/handle/121111/72138
Collection中国科学院化学研究所
Corresponding AuthorPodstawka-Proniewicz, Edyta
Affiliation1.Jagiellonian Univ, Fac Chem, PL-30060 Krakow, Poland
2.Kwansei Gakuin Univ, Sch Sci & Technol, Sanda, Hyogo 6691337, Japan
3.Hankuk Univ Foreign Studies, Dept Chem, Yongin 449791, Kyunggi Do, South Korea
4.Peking Univ, Coll Chem & Mol Engn, Beijing Natl Lab Mol Sci, Beijing 100871, Peoples R China
5.State Higher Vocat Sch, PL-33100 Tarnow, Poland
Recommended Citation
GB/T 7714
Podstawka-Proniewicz, Edyta,Ozaki, Yukihiro,Kim, Younkyoo,et al. Surface-enhanced Raman scattering studies on bombesin, its selected fragments and related peptides adsorbed at the silver colloidal surface[J]. APPLIED SURFACE SCIENCE,2011,257(19):8246-8252.
APA Podstawka-Proniewicz, Edyta,Ozaki, Yukihiro,Kim, Younkyoo,Xu, Yizhuang,&Proniewicz, Leonard M..(2011).Surface-enhanced Raman scattering studies on bombesin, its selected fragments and related peptides adsorbed at the silver colloidal surface.APPLIED SURFACE SCIENCE,257(19),8246-8252.
MLA Podstawka-Proniewicz, Edyta,et al."Surface-enhanced Raman scattering studies on bombesin, its selected fragments and related peptides adsorbed at the silver colloidal surface".APPLIED SURFACE SCIENCE 257.19(2011):8246-8252.
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