2012
DOI: 10.1016/j.bbapap.2012.04.008
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FTIR and XPS studies of protein adsorption onto functionalized bioactive glass

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Cited by 86 publications
(85 citation statements)
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“…For tested SBF amide groups. 64,[66][67][68][70][71][72] In the case of the DCC samples, one can notice a significant increase in the intensity of this component, in good agreement with the N1s findings ( Figure 15A). Therefore, the XPS results confirmed the hypothesis of the formation of an organic screening layer (of amino acid and/or protein nature) that induced latency in the bioactivity process.…”
Section: Discussionsupporting
confidence: 78%
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“…For tested SBF amide groups. 64,[66][67][68][70][71][72] In the case of the DCC samples, one can notice a significant increase in the intensity of this component, in good agreement with the N1s findings ( Figure 15A). Therefore, the XPS results confirmed the hypothesis of the formation of an organic screening layer (of amino acid and/or protein nature) that induced latency in the bioactivity process.…”
Section: Discussionsupporting
confidence: 78%
“…The peaks situated at lower binding energy (ie, ~398.9 eV and 399.9-400.7 eV) were associated with neutral amine and carbon-bonded nitrogen in an amidic bond, respectively. [64][65][66][67][68][69][70][71][72] The peak situated at higher binding energy (~400.3-402.2 eV) pertained to the protonated amine groups. In the case of samples tested in DS (which contained only amino acids), the spectra exhibited only the maxima of amino groups: protonated amino groups at higher binding energy (~400.3 eV), and unprotonated (neutral) amino groups at lower binding energies (~398.9 eV) ( Figure 15A).…”
Section: Discussionmentioning
confidence: 99%
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“…3,39,46 This biopolymer has regions already identified as amide I, between 1,700-1,600 cm, , due to the deformation of CH 2 and CH 3 ; amide II between 1,600-1,500 cm -1 , due to C = N stretching and N = H deformation, and amide III between 1,300-1,180 cm -1 , by the C-N stretching and N-H deformation, which are the main components in the formation of tissue repair. 3,34,35 At 7 days, the spectra were similar for all treatment groups compared with the control. However, at 14 days, the LED + D group had higher amounts of type I collagen (higher a-helix value) and more organized collagenous fibers, confirming the results of the histological analysis.…”
Section: Discussionmentioning
confidence: 67%
“…To identify the main vibrational bands contributions, the spectra were divided in seven regions and the band assignments are shown in Table 1. 3,26,[32][33][34][35][36][37][38] The spectral second derivatives were performed at an experimental time of 14 days, as depicted in Fig. 6.…”
Section: Morphometric Analysismentioning
confidence: 99%