Vibrational Study on Structure and Bioactivity of Protein Fibers Grafted with Phosphorylated Methacrylates
In the last decades, silk fibroin and wool keratin have been considered functional materials for biomedical applications. In this study, fabrics containing silk fibers from <i>Bombyx mori</i> and Tussah silk fibers from <i>Antheraea pernyi</i>, as well as wool keratin fabrics...
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oai:doaj.org-article:face50b3e4c948558c599bac74d0dc6d2021-11-11T18:29:11ZVibrational Study on Structure and Bioactivity of Protein Fibers Grafted with Phosphorylated Methacrylates10.3390/molecules262164871420-3049https://doaj.org/article/face50b3e4c948558c599bac74d0dc6d2021-10-01T00:00:00Zhttps://www.mdpi.com/1420-3049/26/21/6487https://doaj.org/toc/1420-3049In the last decades, silk fibroin and wool keratin have been considered functional materials for biomedical applications. In this study, fabrics containing silk fibers from <i>Bombyx mori</i> and Tussah silk fibers from <i>Antheraea pernyi</i>, as well as wool keratin fabrics, were grafted with phosmer CL and phosmer M (commercial names, i.e., methacrylate monomers containing phosphate groups in the molecular side chain) with different weight gains. Both phosmers were recently proposed as flame retarding agents, and their chemical composition suggested a possible application in bone tissue engineering. IR and Raman spectroscopy were used to disclose the possible structural changes induced by grafting and identify the most reactive amino acids towards the phosmers. The same techniques were used to investigate the nucleation of a calcium phosphate phase on the surface of the samples (i.e., bioactivity) after ageing in simulated body fluid (SBF). The phosmers were found to polymerize onto the biopolymers efficiently, and tyrosine and serine underwent phosphorylation (monitored through the strengthening of the Raman band at 1600 cm<sup>−1</sup> and the weakening of the Raman band at 1400 cm<sup>−1</sup>, respectively). In grafted wool keratin, cysteic acid and other oxidation products of disulphide bridges were detected together with sulphated residues. Only slight conformational changes were observed upon grafting, generally towards an enrichment in ordered domains, suggesting that the amorphous regions were more prone to react (and, sometimes, degrade). All samples were shown to be bioactive, with a weight gain of up to 8%. The most bioactive samples contained the highest phosmers amounts, i.e., the highest amounts of phosphate nucleating sites. The sulphate/sulphonate groups present in grafted wool samples appeared to increase bioactivity, as shown by the five-fold increase of the IR phosphate band at 1040 cm<sup>−1</sup>.Michele Di FoggiaMasuhiro TsukadaPaola TaddeiMDPI AGarticlesilk fibroin<i>Bombyx mori</i>Tussahwool keratingraftingphosmerOrganic chemistryQD241-441ENMolecules, Vol 26, Iss 6487, p 6487 (2021) |
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silk fibroin <i>Bombyx mori</i> Tussah wool keratin grafting phosmer Organic chemistry QD241-441 |
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silk fibroin <i>Bombyx mori</i> Tussah wool keratin grafting phosmer Organic chemistry QD241-441 Michele Di Foggia Masuhiro Tsukada Paola Taddei Vibrational Study on Structure and Bioactivity of Protein Fibers Grafted with Phosphorylated Methacrylates |
description |
In the last decades, silk fibroin and wool keratin have been considered functional materials for biomedical applications. In this study, fabrics containing silk fibers from <i>Bombyx mori</i> and Tussah silk fibers from <i>Antheraea pernyi</i>, as well as wool keratin fabrics, were grafted with phosmer CL and phosmer M (commercial names, i.e., methacrylate monomers containing phosphate groups in the molecular side chain) with different weight gains. Both phosmers were recently proposed as flame retarding agents, and their chemical composition suggested a possible application in bone tissue engineering. IR and Raman spectroscopy were used to disclose the possible structural changes induced by grafting and identify the most reactive amino acids towards the phosmers. The same techniques were used to investigate the nucleation of a calcium phosphate phase on the surface of the samples (i.e., bioactivity) after ageing in simulated body fluid (SBF). The phosmers were found to polymerize onto the biopolymers efficiently, and tyrosine and serine underwent phosphorylation (monitored through the strengthening of the Raman band at 1600 cm<sup>−1</sup> and the weakening of the Raman band at 1400 cm<sup>−1</sup>, respectively). In grafted wool keratin, cysteic acid and other oxidation products of disulphide bridges were detected together with sulphated residues. Only slight conformational changes were observed upon grafting, generally towards an enrichment in ordered domains, suggesting that the amorphous regions were more prone to react (and, sometimes, degrade). All samples were shown to be bioactive, with a weight gain of up to 8%. The most bioactive samples contained the highest phosmers amounts, i.e., the highest amounts of phosphate nucleating sites. The sulphate/sulphonate groups present in grafted wool samples appeared to increase bioactivity, as shown by the five-fold increase of the IR phosphate band at 1040 cm<sup>−1</sup>. |
format |
article |
author |
Michele Di Foggia Masuhiro Tsukada Paola Taddei |
author_facet |
Michele Di Foggia Masuhiro Tsukada Paola Taddei |
author_sort |
Michele Di Foggia |
title |
Vibrational Study on Structure and Bioactivity of Protein Fibers Grafted with Phosphorylated Methacrylates |
title_short |
Vibrational Study on Structure and Bioactivity of Protein Fibers Grafted with Phosphorylated Methacrylates |
title_full |
Vibrational Study on Structure and Bioactivity of Protein Fibers Grafted with Phosphorylated Methacrylates |
title_fullStr |
Vibrational Study on Structure and Bioactivity of Protein Fibers Grafted with Phosphorylated Methacrylates |
title_full_unstemmed |
Vibrational Study on Structure and Bioactivity of Protein Fibers Grafted with Phosphorylated Methacrylates |
title_sort |
vibrational study on structure and bioactivity of protein fibers grafted with phosphorylated methacrylates |
publisher |
MDPI AG |
publishDate |
2021 |
url |
https://doaj.org/article/face50b3e4c948558c599bac74d0dc6d |
work_keys_str_mv |
AT micheledifoggia vibrationalstudyonstructureandbioactivityofproteinfibersgraftedwithphosphorylatedmethacrylates AT masuhirotsukada vibrationalstudyonstructureandbioactivityofproteinfibersgraftedwithphosphorylatedmethacrylates AT paolataddei vibrationalstudyonstructureandbioactivityofproteinfibersgraftedwithphosphorylatedmethacrylates |
_version_ |
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