B2 bradykinin receptor antagonists: adsorption mechanism on electrochemically roughened Ag substrate

• Published in: Journal of Raman spectroscopy Vol. 44; no. 2; pp. 205 - 211
• Main Authors: Proniewicz, Edyta, Skołuba, Dominika, Kudelski, Andrzej, Sobolewski, Dariusz, Prahl, Adam, Kim, Younkyoo, Proniewicz, Leonard M.
• Format: Journal Article
• Language: English
• Published: Bognor Regis Blackwell Publishing Ltd 01.02.2013; Wiley Subscription Services, Inc
• Subjects: bradykinin; receptor antagonist; surface-enhanced Raman scattering
• ISSN: 0377-0486; 1097-4555
• DOI: 10.1002/jrs.4182

In this paper, the surface‐enhanced Raman scattering (SERS) spectra of the potent B2 bradykinin receptor antagonists, [D‐Arg0,Hyp3,Thi5,8,L‐Pip7]BK, Aaa[D‐Arg0,Hyp3,Thi5,8,L‐Pip7]BK, [D‐Arg0,Hyp3,Thi5,D‐Phe7,L‐Pip8]BK, and Aaa[D‐Arg0,Hyp3,Thi5,D‐Phe7,L‐Pip8]BK, were measured when immobilized onto a highly specific electrochemically roughened SERS‐active Ag substrate characterized by the formation of a 50 – 150 nm Ag islands on its surface. The observed SERS bands corresponding to different vibrational modes of the molecule, attached to or near Ag, and the variations in these bands resulting from competitive interactions of the functional groups of the peptides with the SERS‐active Ag surfaces and reorientation occurring over time of adsorption were analyzed in this study. Copyright © 2012 John Wiley & Sons, Ltd. In this paper, the surface‐enhanced Raman scattering (SERS) spectra of the potent B2 bradykinin receptor antagonists, [D‐Arg0,Hyp3,Thi5,8,L‐Pip7]BK, Aaa[D‐Arg0,Hyp3,Thi5,8, L‐Pip7]BK, [D‐Arg0,Hyp3,Thi5,D‐Phe7,L‐Pip8]BK, and Aaa[D‐Arg0,Hyp3,Thi5,D‐Phe7,L‐Pip8]BK, were measured when immobilized onto a highly specific electrochemically roughened SERS‐active Ag substrate characterized by the formation of a 50 – 150 nm Ag islands on its surface. The observed SERS bands corresponding to different vibrational modes of the molecule, attached to or near Ag, and the variations in these bands resulting from competitive interactions of the functional groups of the peptides with the SERS‐active Ag surfaces and reorientation occurring over time of adsorption were analyzed in this study.