Metallic nanoparticles as effective sensors of bio-molecules.

This work describes biologically important nanostructures of metals (AgNPs, AuNPs, and PtNPs) and metal oxides (Cu2ONPs, CuONSs, γ-Fe2O3NPs, ZnONPs, ZnONPs-GS, anatase-TiO2NPs, and rutile-TiO2NPs) synthesized by different methods (wet-chemical, electrochemical, and green-chemistry methods). The nanostructures were characterized by molecular spectroscopic methods, including scanning/transmission electron microscopy (SEM/TEM), energy dispersive X-ray spectroscopy (EDS), X-ray diffraction analysis (XRD), photoelectron spectroscopy (XPS), ultraviolet-visible spectroscopy (UV-vis), dynamic light scattering (DLS), Raman scattering spectroscopy (RS), and infrared light spectroscopy (IR). Then, a peptide (bombesin, BN) was adsorbed onto the surface of these nanostructures from an aqueous solution with pH of 7 that did not contain surfactants. Adsorption was monitored using surface-enhanced Raman scattering spectroscopy (SERS) to determine the influence of the nature of the metal surface and surface evolution on peptide geometry. Information from the SERS studies was compared with information on the biological activity of the peptide. The SERS enhancement factor was determined for each of the metallic surfaces.

Is the Use of Surface-Enhanced Infrared Spectroscopy Justified in the Selection of Peptide Fragments That Play a Role in Substrate-Receptor Interactions? Adsorption of Amino Acids and Neurotransmitters on Colloidal Ag and Au Nanoparticles.

This paper describes an application of attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) and surface-enhanced infrared spectroscopy (SEIRA) to characterize the selective adsorption of four peptides present in body fluids such as neuromedin B (NMB), bombesin (BN), neurotensin (NT), and bradykinin (BK), which are known as markers for various human carcinomas. To perform a reliable analysis of the SERIA spectra of these peptides, curve fitting of these spectra in the spectral region above 1500 cm-1 and SEIRA measurements of sulfur-containing and aromatic amino acids were performed. On the basis of the analyses of the spectral profiles, specific conclusions were drawn regarding specific molecule-metal interactions and changes in the interaction during the substrate change from the surface of silver nanoparticles (AgNPs) to gold nanoparticles (AuNPs).

Adsorption of (Phe-h5)/(Phe-d5)-substituted peptides from neurotensin family on the nanostructured surfaces of Ag and Cu: SERS studies.

This work describes an application of Raman (RS) and surface-enhanced Raman scattering (SERS) to characterize the selective adsorption of two peptides belonging to the neurotensin family peptides, such as kinetensin (KN) and xenopsin-related peptide 2 (XP-2) that are known to stimulate the growth of human tumors. To perform a reliable analysis of SERS spectra, the L-Phe residue (at position 8 or 1 in the amino acid sequence of these peptides) was replaced with L-Phe-d5 (five protons of L-phenylalanine ring substituted by deuterium). Native and (Phe-d5)-isotopically labeled peptides were deposited on electrochemically nanostructured surfaces of Ag (AgORC) and Cu (CuORC) from an aqueous solution (H2O). To determine the share of amide bonds in the interaction with the metallic substrate, SERS spectra of peptides adsorbed on AgORC from heavy water (D2O) were measured. Also, to determine the effect of the C-end on the SERS spectrum, measurements were made for the KN analog in which the C-terminal L-leucine was removed ([desLeu9]KN). Based on the analyses of the spectral profiles, in the spectral range of 600-1650 cm-1, specific conclusions have been drawn regarding specific aromatic ring···metal interactions and changes in the interaction during substrate change.

Biological application of water-based electrochemically synthesized CuO leaf-like arrays: SERS response modulated by the positional isomerism and interface type.

Cupric oxide leaf-like nanostructures (CuONSs) (average dimensions: 80-180 nm in width and 400-750 nm in length) were synthesized via anodic electrochemical dissolution of copper in an ethanol solution containing LiCl electrolyte and water. Ultraviolet-visible (UV-Vis), Fourier-transform infrared (FT-IR), and Raman spectroscopies as well as scanning electron microscope (SEM), high-resolution transmission electron microscopy with energy dispersive X-ray (HD-TEM-EDS), X-ray photoelectron spectroscopy (XPS), and X-ray powder diffraction (XRD) were used to explore the metal surface plasmon, size, rheology, and structure of CuONSs. Then, pyridine α-aminophosphinic acid isomers (α-, ß-, and γ-NHPy) were synthesized and assembled on the CuONS/air and CuONS/aqueous solution interfaces at the pH level of solution = 7. Differences in adsorption and thus in the spectral response resulting from positional isomerism were examined by surface-enhanced Raman scattering (SERS) with an excitation wavelength of 785 nm. The manner of interaction of the investigated isomers with CuONSs in an aqueous solution was discussed in detail and compared with that at the CuONS/air interface. For γ-NHPy, at the CuONS/water interface, the time-dependent changes in the spectral profile were observed and analyzed. For ß-NHPy at the CuONS/air interface, tip-enhanced Raman scattering (TERS) measurements were performed. These measurements allowed observing single molecule behavior and avoiding interference from the molecule's surrounding environment.

Tip-enhanced Raman spectroscopy of bradykinin and its B2 receptor antagonists adsorbed onto colloidal suspended Ag nanowires.

The tip-enhanced Raman scattering (TERS) spectra of bradykinin (BK) and its potent B2 BK receptor antagonists, [d-Arg(0),Hyp(3),Thi(5,8),l-Pip(7)]BK and [d-Arg(0),Hyp(3),Thi(5),d-Phe(7),l-Pip(8)]BK, approximately with a size of about 40 nm, adsorbed onto colloidal suspended Ag nanowires with diameter in the range of 350-500 nm and length of 2-50 µm were recorded. The metal surface plasmon resonance and morphology of the Ag nanowires were studied by ultraviolet-visible (UV-Vis) spectroscopy and scanning electron microscopy (SEM). Briefly, it was shown that two C-terminal amino acids of BK and [d-Arg(0),Hyp(3),Thi(5,8),l-Pip(7)]BK are involved in the interaction with the colloidal suspended Ag nanowire surface, whereas three last amino acids of the [d-Arg(0),Hyp(3),Thi(5),d-Phe(7),l-Pip(8)]BK sequence attached the Ag surface. Thus, BK adsorbs on the colloidal suspended Ag nanowires mainly through the Phe(5/8) ring (tilted orientation) and the one oxygen atom of the carboxylate group and the H2N-C-NH-CH2- fragment of Arg(9). In the case of [d-Arg(0),Hyp(3),Thi(5,8),l-Pip(7)]BK, the Thi(8) ring (through the lone electron pair on the sulfur atom) and the both oxygen atoms of the carboxylate group and the amine group of Arg(9) mainly participated in the interaction with the Ag nanowire surface. For [d-Arg(0),Hyp(3),Thi(5),d-Phe(7),l-Pip(8)]BK, the d-Phe(7) ring, the Pip(8) ring, and the Arg(9) side-chain assisted in the peptide interaction with the Ag surface. The obtained results emphasize the importance of the C-terminal part of these peptides in the adsorption process onto the colloidal suspended Ag nanowires.

Surface- and tip-enhanced Raman scattering of bradykinin onto the colloidal suspended Ag surface.

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.

Nociceptin and its natural and specifically-modified fragments: Structural studies.

The vibrational structures of Nociceptin (FQ), its short bioactive fragments, and specifically-modified [Tyr¹]FQ (1-6), [His¹]FQ (1-6), and [His(1,4)]FQ (1-6) fragments were characterized. We showed that in the solid state, all of the aforementioned peptides except FQ adopt mainly turn and disordered secondary structures with a small contribution from an antiparallel ß-sheet conformation. FQ (1-11), FQ (7-17) [His¹]FQ (1-6), and [His(1,4)]FQ (1-6) have an α-helical backbone arrangement that could also slightly influence their secondary structure. The adsorption behavior of these peptides on a colloidal silver surface in an aqueous solution (pH = ∼8.3) was investigated by means of surface-enhanced Raman scattering (SERS). All of the peptides, excluding FQ (7-17), chemisorbed on the colloidal silver surfaces through a Phe4 residue, which for FQ, FQ (1-11), FQ (1-6), [Tyr¹]FQ (1-6), and [His¹]FQ (1-6) lies almost flat on this surface, while for FQ (1-13) and FQ (1-13)NH2 adopts a slightly tilted orientation with respect to the surface. The Tyr¹ residue in [Tyr¹]FQ (1-6) does not interact with the colloidal silver surface, suggesting that the Tyr¹ and Phe4 side chains are located on the opposite sides of the peptide backbone, which can be also true for His¹ and Phe4 in [His¹]FQ (1-6). The lone pair of electrons on the oxygen atom of the ionized carbonyl group of FQ (1-13) and FQ (7-17) appears to be coordinated to the colloidal silver nanoparticles, whereas in the case of the remaining peptides, it only assists in the adsorption process, similar to the --NH4 group. We also showed that upon adsorption, the secondary structure of these peptides is altered.