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Effects of site-specific phosphorylation on the mechanical properties of ovalbumin-based hydrogels.
- Source :
-
International journal of biological macromolecules [Int J Biol Macromol] 2017 Sep; Vol. 102, pp. 1286-1296. Date of Electronic Publication: 2017 May 08. - Publication Year :
- 2017
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Abstract
- An efficient one-step grafting approach was developed to modify ovalbumin (OVA) by phosphorylation through selective reaction with the hydroxyl group of Ser and Thr residues present in OVA. The site-specific phosphorylated conjugates were characterized by Matrix-Assisted Laser Desorption Ionization-Time-of-Flight Mass Spectrometry (MALDI-TOF/MS) and the results indicated that the Ser residue could be more readily phosphorylated, and the typical phosphopeptides <superscript>264</superscript> LTEWTSSNVMEER <superscript>276</superscript> and <superscript>340</superscript> EVVGSAEAGVDAASVSEEFR <superscript>359</superscript> demonstrated the formation of monophosphoester. Moreover, <superscript>13</superscript> C NMR analysis showed that the βCH <subscript>2</subscript> of Ser acted as a hydroxyl donor to react with sodium tripolyphosphate (STPP), and the conjugates with variable phosphorylation sites could improve the weak network and the resulting poor mechanical properties of ovalbumin-based hydrogels. Furthermore, small-amplitude oscillatory measurements, creep recovery tests and texture profile analysis of hardness and stickiness indicated that phosphorylation can strengthen the intermolecular cross-linking of protein molecules and produce significant influence on the rheological behavior and texture properties, suggesting that a suitable conjugation site is essential for the best gelation properties at a different pH. The integrated results indicate that phosphorylation change significantly modify the viscoelastic and mechanical properties of OVA-based hydrogels by changing molecular dynamics upon heating.<br /> (Copyright © 2017 Elsevier B.V. All rights reserved.)
Details
- Language :
- English
- ISSN :
- 1879-0003
- Volume :
- 102
- Database :
- MEDLINE
- Journal :
- International journal of biological macromolecules
- Publication Type :
- Academic Journal
- Accession number :
- 28495627
- Full Text :
- https://doi.org/10.1016/j.ijbiomac.2017.05.028