SERS, Molecular Dynamics and Molecular Orbital Studies of the MRKDV Peptide on Silver and Membrane Surfaces

Aliaga, Álvaro; Ahumada, Hernán; Sepúlveda, Karen Tapia; Gómez-Jeria, Juan S.; Garrido, C.; Weiss-López, Boris; Campos‐Vallette, Marcelo

doi:10.1021/jp1107153

Cited by 38 publications

(31 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Gaussian software was used . The silver surface was simulated as follows: a large ( a = 0.408 nm) Ag cube with a face‐centered cubic structure was built as in our previous studies . The resulting structure was trimmed to get a planar double layer composed of 324 Ag atoms.…”

Section: Methodsmentioning

confidence: 92%

Proline and hydroxyproline deposited on silver nanoparticles. A Raman, SERS and theoretical study

Cárcamo¹,

Aliaga²,

Clavijo³

et al. 2011

J Raman Spectroscopy

View full text Add to dashboard Cite

The Raman and surface‐enhanced Raman scattering (SERS) spectra of l‐proline (Pro) and trans‐4‐hydroxy‐ l‐proline (Hyp) were recorded. SERS spectra were obtained on colloidal Ag prepared by reduction with hydroxylamine. Allowing sufficient time for Pro and Hyp to adjust in the colloidal solution resulted fundamentally in obtaining unique and reproducible SERS spectra. Hyp stabilizes on the surface more rapidly than Pro. The spectral analysis indicates that Pro interacts with the Ag surface through the carboxylate group. The interaction of Hyp with the metal surface occurs through the amino, methylene and carboxylate moieties of the molecule. The spectroscopic results are supported by quantum chemical calculations, performed using extended Hückel theory (EHT) of the title compounds interacting with an Ag cluster model. The assignment of the Raman bands was supported by a normal coordinate analysis performed through Becke, three‐parameter, Lee–Yang–Parr/6‐311 G* + calculations. Copyright © 2011 John Wiley & Sons, Ltd.

show abstract

Section: Methodsmentioning

confidence: 92%

Proline and hydroxyproline deposited on silver nanoparticles. A Raman, SERS and theoretical study

Cárcamo¹,

Aliaga²,

Clavijo³

et al. 2011

J Raman Spectroscopy

View full text Add to dashboard Cite

show abstract

“…A planar silver surface composed by 800 atoms was built as in our previous works [22][23][24][25] . In the first study, a 4-MPTP molecule was placed on the surface at different distances and orientations.…”

Section: Calculationmentioning

confidence: 99%

Raman and Surface Enhanced Raman Signals of the Sensor 1-(4-Mercaptophenyl)-2,4,6-Triphenylpyridinium Perchlorate

Célis

Campos‐Vallette

Vega

et al. 2015

J. Chil. Chem. Soc.

View full text Add to dashboard Cite

The sensor 1-(4-mercaptophenyl)-2,4,6-triphenylpyridinium perchlorate compound was vibrationally characterized using Raman and the Surface-Enhanced Raman techniques, SERS and Shell-Isolated Nanoparticles-Enhanced Raman Spectroscopy (SHINERS). The Raman spectrum was analyzed and the band assignment was supported using DFT data at the B3LYP/6-31G(d) level. SERS data allowed infer about the orientation of the analyte on the naked Ag surface. EHT calculations for an Ag/analyte model represent well the SERS spectrum supporting the Ag-S bond formation. The SHINERS spectrum was obtained by using Ag@SiO 2 nanoparticles prepared at two different time of the SiO 2 coating process. The most intense SHINERS spectral signals of the compound (100 nM) were obtained after 20 minutes of the Ag@SiO 2 formation. No charge-transfer was concluded from the SHINERS experiments.

show abstract

“…In recent years, substantial progress has been made in understanding adsorption and conformational changes of proteins and peptides on different kinds of surfaces [12][13][14][15][16][17][18][19][20][21][22][23][24][25][26]. Generally, the structural changes of proteins and peptides adsorbed on hydrophilic or charged surfaces are due to long-range electrostatic interactions, while on hydrophobic surfaces, the conformational changes are dominated by strong hydrophobic interactions between nonpolar side chains of amino acids and surface particles.…”

Section: Introductionmentioning

confidence: 99%

Effects of surface hydrophobicity on the conformational changes of polypeptides of different length

Yan

2011

Phys. Rev. E

View full text Add to dashboard Cite

We studied the effects of surface hydrophobicity on the conformational changes of different length polypeptides by calculating the free energy difference between peptide structures using the bias-potential Monte Carlo technique and the probability ratio method. It was found that the hydrophobic surface plays an important role in the stability of secondary structures of the polypeptides with hydrophobic side chains. For short GAAAAG peptides, the hydrophobic surface destabilizes the α helix but stabilizes the β hairpin in the entire temperature region considered in our study. Interestingly, when the surface hydrophobic strength ε(hpsf)≥ε(hp), the most stable structure in the low temperature region changes from α helix to β hairpin, and the corresponding phase transition temperature increases slightly. For longer GAAAAAAAAAAG peptides, the effects of the relatively weak hydrophobic surface (ε(hpsf) < ε(hp)) on α-helical structures may be neglected, while the relatively strongly hydrophobic surface (ε(hpsf)≥ε(hp)) leads to the obvious partial helicity loss. In contrast, the stability of β structures can be enhanced significantly by the hydrophobic surface, especially by the strongly hydrophobic surface, at low and intermediate temperatures. At high temperatures, in addition to thermal fluctuations, the strongly hydrophobic surface (ε(hpsf)>ε(hp)) may further disturb the formation of both α-helical and β structures. Moreover, the phase transition temperature between α-helical structures and random coils significantly decreases due to the helicity loss when ε(hpsf)>ε(hp). Our findings provide a basic and quantitative picture for understanding the effects of a hydrophobic surface on the conformational changes of the polypeptides with hydrophobic side chains. From an application viewpoint, the present study is helpful in developing alternative strategies of producing high-quality biological fibrillar materials and functional nanoscale devices by the self-assembly of the polypeptides on hydrophobic surfaces.

show abstract

SERS, Molecular Dynamics and Molecular Orbital Studies of the MRKDV Peptide on Silver and Membrane Surfaces

Cited by 38 publications

References 45 publications

Proline and hydroxyproline deposited on silver nanoparticles. A Raman, SERS and theoretical study

Proline and hydroxyproline deposited on silver nanoparticles. A Raman, SERS and theoretical study

Raman and Surface Enhanced Raman Signals of the Sensor 1-(4-Mercaptophenyl)-2,4,6-Triphenylpyridinium Perchlorate

Effects of surface hydrophobicity on the conformational changes of polypeptides of different length

Contact Info

Product

Resources

About