Search

In this paper, surface- (SERS) and tip-enhanced Raman scattering (TERS) techniques were used to determine the adsorption mode of bradykinin (BK), a small peptide implicated in, for example, carcinoma growth, onto colloidal suspended Ag surfaces under various environmental conditions, including: peptide concentrations (10(-5)-10(-7) M), excitation wavelengths (514.5 and 785.0 nm), and pH of aqueous sol solutions (from pH = 3 to pH = 11). The metal surface plasmon and rheology of the colloidal suspended Ag surface were explored by ultraviolet-visible (UV-Vis) spectroscopy and atomic force/scanning electron microscopy (AFM/SEM). The SERS results indicated that the peptide concentration of 10(-5) M was the optimal peptide concentration for monolayer colloidal coverage. The Phe(5/8) and Arg(9) residues of BK generally participated in the interactions with colloidal suspended Ag surfaces. The amide group appeared to be arranged in the same manner to the Ag surface in the pH range of 3 to 11. At acidic pH of the solution (pH = 3 to 5), the BK -COO(-) terminal group binds to the Ag surface as a bidentate (at pH = 3) or monodentate (at pH = 5) chelating ligand. At pH = 11, the imino group of Arg(9), probably due to its -C[double bond, length as m-dash]N(⊕)H2 protonation state, was not involved in the interaction with Ag. The reduction in the solution alkalinity (pH = 9) produced the deprotonation of the -C=N(⊕)H2 group followed by group rearrangement in a way favoring the interaction between the lone electron pair on N and Ag. The TERS studies confirmed the proposed, on the basis of SERS, behavior of BK onto the colloidal suspended Ag at pH = 7 and showed that in different points of the colloidal suspended Ag surface the same peptide fragments approximately having the same orientations with respect to this surface interact with it.