Biocompatible Materials Based on Self-Assembling Peptides on Ti25Nb1OZr Alloy: Molecular Structure and Organization Investigated by Synchrotron Radiation Induced Techniques
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F18%3A10389408" target="_blank" >RIV/00216208:11320/18:10389408 - isvavai.cz</a>
Výsledek na webu
<a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=beB2XCqZRK" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=beB2XCqZRK</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/nano8030148" target="_blank" >10.3390/nano8030148</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Biocompatible Materials Based on Self-Assembling Peptides on Ti25Nb1OZr Alloy: Molecular Structure and Organization Investigated by Synchrotron Radiation Induced Techniques
Popis výsledku v původním jazyce
In this work, we applied advanced Synchrotron Radiation (SR) induced techniques to the study of the chemisorption of the Self Assembling Peptide EAbuK16, i.e., H-Abu-Glu-Abu-Glu-Abu-Lys-Abu-Lys-Abu-Glu-Abu-Glu-Abu-Lys-Abu-Lys-NH2 that is able to spontaneously aggregate in anti-parallel P-sheet conformation, onto annealed Ti25NblOZr alloy surfaces. This synthetic amphiphilic oligopeptide is a good candidate to mimic extracellular matrix for bone prosthesis, since its beta-sheets stack onto each other in a multilayer oriented nanostructure with internal pores of 5-200 nm size. To prepare the biomimetic material, Ti25NblOZr discs were treated with aqueous solutions of EAbuK16 at different pH values. Here we present the results achieved by performing SR-induced X-ray Photoelectron Spectroscopy (SR-XPS), angle-dependent Near Edge X-ray Absorption Fine Structure (NEXAFS) spectroscopy, FESEM and AFM imaging on Ti25NblOZr discs after incubation with self-assembling peptide solution at five different pH values, selected deliberately to investigate the best conditions for peptide immobilization.
Název v anglickém jazyce
Biocompatible Materials Based on Self-Assembling Peptides on Ti25Nb1OZr Alloy: Molecular Structure and Organization Investigated by Synchrotron Radiation Induced Techniques
Popis výsledku anglicky
In this work, we applied advanced Synchrotron Radiation (SR) induced techniques to the study of the chemisorption of the Self Assembling Peptide EAbuK16, i.e., H-Abu-Glu-Abu-Glu-Abu-Lys-Abu-Lys-Abu-Glu-Abu-Glu-Abu-Lys-Abu-Lys-NH2 that is able to spontaneously aggregate in anti-parallel P-sheet conformation, onto annealed Ti25NblOZr alloy surfaces. This synthetic amphiphilic oligopeptide is a good candidate to mimic extracellular matrix for bone prosthesis, since its beta-sheets stack onto each other in a multilayer oriented nanostructure with internal pores of 5-200 nm size. To prepare the biomimetic material, Ti25NblOZr discs were treated with aqueous solutions of EAbuK16 at different pH values. Here we present the results achieved by performing SR-induced X-ray Photoelectron Spectroscopy (SR-XPS), angle-dependent Near Edge X-ray Absorption Fine Structure (NEXAFS) spectroscopy, FESEM and AFM imaging on Ti25NblOZr discs after incubation with self-assembling peptide solution at five different pH values, selected deliberately to investigate the best conditions for peptide immobilization.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10305 - Fluids and plasma physics (including surface physics)
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2018
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Nanomaterials
ISSN
2079-4991
e-ISSN
—
Svazek periodika
8
Číslo periodika v rámci svazku
3
Stát vydavatele periodika
CH - Švýcarská konfederace
Počet stran výsledku
19
Strana od-do
148
Kód UT WoS článku
000428106800020
EID výsledku v databázi Scopus
2-s2.0-85044793221