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Surface-enhanced Raman scattering studies on bombesin, its selected fragments and related peptides adsorbed at the silver colloidal surface
Podstawka-Proniewicz, Edyta ; Ozaki, Yukihiro ; Kim, Younkyoo ; Xu, Yizhuang ; Proniewicz, Leonard M.
2011
关键词Surface-enhanced Raman scattering SERS Colloidal silver surface Bombesin BN BN-related peptides GASTRIN-RELEASING-PEPTIDE S STRETCHING VIBRATIONS CELL LUNG-CANCER AMINO-ACIDS BRONCHOPULMONARY DYSPLASIA MOLECULAR-CONFORMATIONS MODIFIED ANALOGS TUMOR-CELLS SPECTROSCOPY RECEPTOR
英文摘要SERS 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.; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000291478000017&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; Chemistry, Physical; Materials Science, Coatings & Films; Physics, Applied; Physics, Condensed Matter; SCI(E); EI; CPCI-S(ISTP); 7
语种英语
DOI标识10.1016/j.apsusc.2011.02.012
内容类型其他
源URL[http://ir.pku.edu.cn/handle/20.500.11897/238830]  
专题化学与分子工程学院
推荐引用方式
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. 2011-01-01.
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