Thin films of a self-assembling peptide on TiO2 and Au studied by NEXAFS, XPS and IR spectroscopies

Polzonetti, Giovanni; Battocchio, Chiara; Iucci, Giovanna; Dettin, Monica; Gambaretto, Roberta; Bello, Carlo Di; Carravetta, Vincenzo

doi:10.1016/j.msec.2005.09.062

Cited by 50 publications

(80 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…XPS investigations were performed on thick films deposited on gold, considered as reference 'bulk' systems, and on thinner films immobilised on TiO 2 . Interpretation of peptide XPS spectra has been thoroughly discussed [5] ; only a short summary will be presented here.…”

Section: Resultsmentioning

confidence: 99%

“…Figure 3 (a) and (b) shows the C1s and N1s spectra of Pept3 deposited on Au. The C1s signal can be resolved by curve-fitting analysis into three components labelled C1-C3 in increasing BE order and corresponding respectively to aliphatic C-C carbons (C1, BE = 285.0 eV), to C-N carbons of the peptide backbone and of the lysine/ornithine pending groups (C2, 286.3 eV), to peptidic carbons and to carboxyls from the glutamate/aspartate pending groups (C3, 288.5 eV) [5,12] ; measured C1/C2/C3 ratios (Table 1) are in agreement with calculated values. In the N1s spectrum ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…3(b)), the main peak (N1) has a BE = 400.0 eV, as expected for peptidic nitrogens, with a shoulder (N2, 402.0 eV) related to protonated nitrogens of the lysine/ornithine pending groups. [5,8] Upon peptide adsorption on TiO 2 , no significant changes were evidenced in the C1s and N1s spectra, suggesting that chemisorption takes place without substantial modifications of the peptide structure. Measured atomic ratios (C/N and C1/C2/C3, Table 1) show a fairly good agreement with the expected values; for Pept2 the C1/C3 ratio is slightly higher than expected, probably due to weak surface contamination.…”

Section: Resultsmentioning

confidence: 99%

“…[5] Titanium, always oxidised to TiO 2 on the outermost surface, is a well-known biocompatible material, widely used in orthopaedic/dental medicine, a fact that has stimulated research on surface modifications aimed at improving its biocompatibility by biomolecules immobilisation. NEXAFS investigations revealed an ordered structure of the peptide backbones on both substrates, with a tilt angle of about 75…”

Section: Introductionmentioning

confidence: 99%

“…Peptides were immobilised on TiO 2 by incubation in aqueous solution, [7] according to the procedure followed for EAK16. [5] Peptide films on Au/Si(111) were prepared by casting from (∼1 mM) aqueous solution and drying in vacuum.…”

mentioning

confidence: 99%

See 4 more Smart Citations

A NEXAFS and XPS study of the adsorption of self‐assembling peptides on TiO₂: the influence of the side chains

Iucci

Battocchio

Dettin

et al. 2008

Surface & Interface Analysis

View full text Add to dashboard Cite

aPeptides consisting of an alternation of hydrophobic and hydrophilic (positively and negatively charged) amino acids can generate extended ordered structures by self-assembling (SA) from aqueous solutions. In this paper we present XPS, near-edge X-ray absorption fine structure (NEXAFS) and Fourier transform infrared (FTIR) investigations on a series of SA peptides with the aim of determining the effect of side-chain length on molecular arrangement and orientation.Peptides were immobilised on the surface of titanium, a well-known biocompatible material, or deposited as thick films on inert gold surfaces. FTIR analysis yields information on the backbone conformation. XPS spectroscopy was used to investigate the peptide adsorption on the TiO 2 surface. The orientation of the peptide chains was investigated by angular-dependent NEXAFS.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

A NEXAFS and XPS study of the adsorption of self‐assembling peptides on TiO₂: the influence of the side chains

Iucci

Battocchio

Dettin

et al. 2008

Surface & Interface Analysis

View full text Add to dashboard Cite

show abstract

Biomimetic peptide‐enriched electrospun polymers: A photoelectron and infrared spectroscopy study

Iucci

Ghezzo

Danesin

et al. 2011

J of Applied Polymer Sci

Self Cite

View full text Add to dashboard Cite

Biomimetic polymer nanofibers of poly(ecaprolactone) and poly(L-lactide-caprolactone) copolymer were prepared by electrospinning. Modifications of the polymer nanofibers aimed at improving their biomimetic properties were performed by two different routes: (1) immobilization of an adhesion peptide, which mimicked the adhesion sequence of the extracellular matrix protein fibronectin, on the polymer surface and (2) incorporation of self-complementary oligopeptides, which showed alternated hydrophilic and hydrophobic side chain groups and was capable of generating extended ordered structures by self-assembling, into the polymer nanofibers. The structure of the polymer/peptide nanofibers was investigated by X-ray photoelectron and Fourier transform infrared spectroscopies.

show abstract

Bioderived Freestanding Film as a Robust Interfacial Protective Layer for Advanced Lithium Metal Anodes

Yang

Chen

et al. 2023

Energy Tech

View full text Add to dashboard Cite

Lithium metal is a potential candidate for anode material in next‐generation rechargeable batteries with high energy and power densities. However, the huge volume change caused by the uneven deposition of metallic Li leads to the cracking of the solid electrolyte interphase (SEI), which cannot prevent the reaction of inner fresh Li with electrolyte, resulting in severe dendrite growth and electrochemical degradation. Herein, a freestanding protein film derived from eggshell is reported as the protective layer on the electrode surface to form a robust artificial SEI layer. Benefiting from its 3D interconnected fiber framework along with good mechanical stiffness and softness, the Li‐ion flow is uniformly modulated, leading to the suppression of Li dendrite growth. The electrochemical performance of corresponding symmetric, asymmetric, and full cells is significantly enhanced. A high coulombic efficiency above 95% for nearly 700 cycles is achieved for the modified Cu/Li asymmetric cell at a current density of 3 mA cm−2 (with a capacity of 1 mAh cm−2). This study indicates a SEI reinforcement approach for the stabilization of the Li metal anode based on the freestanding structure derived from biomaterials.

show abstract

Thin films of a self-assembling peptide on TiO2 and Au studied by NEXAFS, XPS and IR spectroscopies

Cited by 50 publications

References 12 publications

A NEXAFS and XPS study of the adsorption of self‐assembling peptides on TiO₂: the influence of the side chains

A NEXAFS and XPS study of the adsorption of self‐assembling peptides on TiO₂: the influence of the side chains

Biomimetic peptide‐enriched electrospun polymers: A photoelectron and infrared spectroscopy study

Bioderived Freestanding Film as a Robust Interfacial Protective Layer for Advanced Lithium Metal Anodes

Contact Info

Product

Resources

About

Thin films of a self-assembling peptide on TiO2 and Au studied by NEXAFS, XPS and IR spectroscopies

Cited by 50 publications

References 12 publications

A NEXAFS and XPS study of the adsorption of self‐assembling peptides on TiO2: the influence of the side chains

A NEXAFS and XPS study of the adsorption of self‐assembling peptides on TiO2: the influence of the side chains

Biomimetic peptide‐enriched electrospun polymers: A photoelectron and infrared spectroscopy study

Bioderived Freestanding Film as a Robust Interfacial Protective Layer for Advanced Lithium Metal Anodes

Contact Info

Product

Resources

About

A NEXAFS and XPS study of the adsorption of self‐assembling peptides on TiO₂: the influence of the side chains

A NEXAFS and XPS study of the adsorption of self‐assembling peptides on TiO₂: the influence of the side chains