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The tip-enhanced Raman scattering (TERS) spectra of bradykinin (BK) and its potent B2 BK receptor antagonists, [d-Arg0,Hyp3,Thi5,8,l-Pip7]BK and [d-Arg0,Hyp3,Thi5,d-Phe7,l-Pip8]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-Arg0,Hyp3,Thi5,8,l-Pip7]BK are involved in the interaction with the colloidal suspended Ag nanowire surface, whereas three last amino acids of the [d-Arg0,Hyp3,Thi5,d-Phe7,l-Pip8]BK sequence attached the Ag surface. Thus, BK adsorbs on the colloidal suspended Ag nanowires mainly through the Phe5/8 ring (tilted orientation) and the one oxygen atom of the carboxylate group and the H2N–C–NH–CH2– fragment of Arg9. In the case of [d-Arg0,Hyp3,Thi5,8,l-Pip7]BK, the Thi8 ring (through the lone electron pair on the sulfur atom) and the both oxygen atoms of the carboxylate group and the amine group of Arg9 mainly participated in the interaction with the Ag nanowire surface. For [d-Arg0,Hyp3,Thi5,d-Phe7,l-Pip8]BK, the d-Phe7 ring, the Pip8 ring, and the Arg9 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. [ABSTRACT FROM AUTHOR]

This study focuses on the adsorption process of L-cysteine (Cys), a sulfur-containing amino acid, onto monolayers of gold nanoparticles (AuNPs) prepared through distinct protocols on mica substrates. Two types of AuNPs were prepared using two different methods: the first employed a physical approach, which combined the Inert Gas Condensation (IGC) technique with the magnetron sputtering method, while the second utilized a chemical method involving the reduction of tetrachloroauric acid with trisodium citrate (TC). The characterization of AuNPs was performed using transmission electron microscopy (TEM) and atomic force microscopy (AFM), of up to 5 ± 1.3 nm for bare AuNPs obtained through vacuum techniques, and up to 12 ± 5 nm for negatively charged, citrate-stabilized TCAuNPs(-). The application of spectroscopic techniques based on the surface-enhanced effects allows for describing the adsorption process in both micro- and nanoscale systems: Cys/bare AuNPs and Cys/ TCAuNPs(-). The commonly used surface-enhanced Raman spectroscopy (SERS) technique provided insights into adsorption behaviours at the microscale level. In the case of TCAuNPs(-), an interaction involving the lone electron pair of sulfur (S) atom and metal surface, while on the bare AuNPs, S is adsorbed on the surface, but the cleavage of the SH group is not discernible. Nanoscale analysis was complemented using AFM combined with the surface-enhanced infrared absorption spectroscopy (AFM-SEIRA) technique. AFM-SEIRA map indicated the formation of hot spot which were predominantly located between aggregated TCAuNPs(-) and on specific NPs surfaces (area between NPs and gold-coated tip). Results from the SERS and AFM-SEIRA techniques were in good agreement, underscoring the comprehensive understanding achieved through the chosen experimental approach regarding the Cys interactions with layers of AuNPs., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

In this study, the corrosion inhibition performance of the natural polysaccharide guar gum (GG) for N80 carbon steel in CO 2 -saturated saline solution at different temperatures and immersion times was investigated by weight loss and electrochemical measurements. The results have revealed that GG showed good inhibition performance at lower and higher temperatures. The inhibition efficiency observed via weight loss measurements reached 76.16 and 63.19% with 0.4 g L -1 of GG, at 25 and 50 °C, respectively. The inhibition efficiency of GG increased as the inhibitor concentration and immersion time increased but decreased with increasing temperature. EIS measurements have shown that, even after prolonged exposure, GG was still able to protect the metal surface. Potentiodynamic measurements showed the mixed-type nature of GG inhibitive action. The Temkin and Dubinin-Radushkevich adsorption isotherm models give accurate fitting of the estimated data, and the calculated parameters indicated that the adsorption of GG occurred mainly via an electrostatic or physical adsorption process. The associated activation energy ( E a ) and the heat of adsorption ( Q a ) supported the physical adsorption nature of GG. FTIR analysis was used to explain the adsorption interaction between the inhibitor and the N80 carbon steel surface. SEM-EDS and AFM confirmed the adsorption of GG and the formation of an adsorptive layer of GG on the metal surface.

The work presents a comprehensive vibrational analysis of the process of adsorption of threonine (Thr) onto an Fe surface with deposited Cu nanoparticles (NPs) (of about 4-5 nm in size) in a corrosive environment. The application of surface-enhanced Raman spectroscopy (SERS) and surface-enhanced infrared absorption spectroscopy (SEIRA) provides the opportunity for detailed description of adsorption geometry of amino acid onto a metal surface. The combination of conventional infrared spectroscopy (IR) with atomic force microscopy (AFM) resulted in a nano-SEIRA technique which made it possible to provide a precise description of adsorbate binding to the metal surface. The studies presented confirmed that there is a very good correlation between the spectra recorded by the SERS, SEIRA, and nano-SEIRA techniques. Threonine significantly influenced the process of corrosion of the investigated surface due to the existing strong interaction between the protonated amine and carboxylate groups and the CuNPs deposited onto the Fe surface. In addition, the application of two polarization modulations ( s and p ) in nano-SEIRA allows subtle changes to be observed in the molecule geometry upon adsorption, with the carboxylate group of Thr being almost horizontally oriented onto the metal surface; whereas the amine group that contains nitrogen is oriented perpendicular to this surface.

It has been suggested that the family of neuropeptide Y (NPY) peptides is a promising target for the neuroprotective therapy; therefore, knowledge of the structure of these biologically active compounds and their behavior at solid/liquid interface is important in order to design new analogues. Because there is still a lack of detailed information on the behavior of NPY and its mutated analogues at the solid/liquid interfaces, in this work surface-enhanced Raman spectroscopy (SERS) analysis was used to investigate NPY and its native NPY 3-36 , NPY 13-36 , and NPY 22-36 and mutated acetyl-(Leu 28,31 )-NPY 24-36 C-terminal fragments, acting on Y 2 receptors (Y 2 R), in order to determine their possible metal surface/molecule interactions. In these studies, colloidal gold nanoparticle surface served as a solid surface, whereas an aqueous solution was used as a liquid medium. The observed differences in the band intensities, wavenumbers, and widths allowed us to draw conclusions on an adsorption mode of NPY and on changes in this mode upon the shortening of the peptide chain and increase in solution pH (from pH 3 to pH 11). Briefly, three different species of Tyr were identified onto the colloidal gold surface depending upon the length of the peptide chain and solution pH. Tyrosine (TyrOH) is present in a basic medium. Tyrosinate (TyrO - ) is present in an acidic solution, whereas phenoxyl radical (Tyr * ) appears at neutral pH for peptides having relatively short peptide chain (acetyl-(Leu 28,31 )-NPY 24-36 ). The elongation of the peptide chain partially (NPY 13-36 and NPY 22-36 ) or completely (NPY 3-36 and NPY) protects the Tyr residue against conversion to the radical form., (Copyright © 2016 Elsevier B.V. All rights reserved.)

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.

In this paper, we present spectroscopic studies of neuropeptide Y (NPY) and its native NPY(3-36), NPY(13-36), and NPY(22-36) and mutated acetyl-(Leu(28,31))-NPY(24-36)C-terminal fragments acting on Y2 receptor. Since there is some evidence for the correlation between the SERS patterns and the receptor binding ability, we performed a detailed analysis for these compounds at the metal/water interface using Raman spectroscopy (RS) and surface-enhanced Raman spectroscopy (SERS) methods. Many studies have suggested that interactions of this kind are crucial for a variety of biomedical and biochemical phenomena. The identification of amino acids in these peptide sequences by SERS allowed us to determine which molecular fragments were responsible for the interaction with the silver nanoparticle surface. Our findings demonstrated that in all of the investigated compounds, the NPY(32-36)C-terminal fragment (Thr(32)-Arg(33)-Gln(34)-Arg(35)-Tyr(36)NH2) was involved in the adsorption process onto metal substrate. The results of the present study suggest that the same molecular fragment interacts with the Y2 receptor, what proved the usefulness of the SERS method in the study of these biologically active compounds. The search for analogs acting on Y2 receptor may be important from the viewpoint of possible future clinical applications., (Copyright © 2014 Elsevier Inc. All rights reserved.)