Theoretical pKa prediction of O-phosphoserine in aqueous solution

Śmiechowski, Maciej

doi:10.1016/j.cplett.2010.10.063

Cited by 30 publications

(20 citation statements)

References 42 publications

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“…More pronounced phospho‐content results in decreased swelling. Since the phospho‐group of Ser has a pkA 1 of 2.19 and pkA 2 of 5.78 [63], the double negative charge will be present on modified Ser at neutral and basic pH. This fact explains why the swelling ratio of films is greater at basic pH, but not acidic pH.…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: A platform for the production of tuneable material

Volkov

Vasconcelos

Sárria

et al. 2014

Biotechnology Journal

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Silk fibroin demonstrates great biocompatibility and is suitable for many biomedical applications, including tissue engineering and regenerative medicine. Current research focuses on manipulating the physico-chemical properties of fibroin, and examining the effect of this manipulation on firobin's biocompatibility. Regenerated silk fibroin was modified by in vitro enzymatic phosphorylation and cast into films. Films were produced by blending, at several ratios, the phosphorylated and un-phosphorylated fibroin solutions. Fourier transform infra-red spectroscopy was used to determine the specific P-OH vibration peak, confirming the phosphorylation of the regenerated silk fibroin solution. Differential scanning calorimetry showed that phosphorylation altered the intra- and inter-molecular interactions. Further experiments demonstrated that phosphorylation can be used to tailor the hydrophylicity/hydrophobicity ratio as well as the crystalinity of silk fibroin films. Release profiling of a model drug was highly dependent on silk modification level. Cytotoxicity assays showed that exposure to lixiviates of phosphorylated films only slightly affected cellular metabolism and proliferation, although direct contact resulted in a strong direct correlation between phosphorylation level and cell proliferation. This new method for tuning silk biomaterials to obtain specific structural and biochemical features can be adapted for a wide range of applications. Phosphorylation of silk fibroins may be applied to improve the cytocompatibility of any silk-based device that is considered to be in contact with live animals or human tissues.

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Section: Discussionmentioning

confidence: 99%

Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: A platform for the production of tuneable material

Volkov

Vasconcelos

Sárria

et al. 2014

Biotechnology Journal

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“…3 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 Scheme 2. P-Ser dissociation scheme [30]. matter in the samples after sorption experiment at initial pH 2, detected by TA ( Fig.…”

Section: Discussionmentioning

confidence: 99%

“…The electric tension and the stability of Ca-P-Ser soluble complexes decrease at higher pH values, when the stability of Cu complexes increases [30,31]. 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60…”

Section: Discussionmentioning

confidence: 99%

Dependence of the interaction mechanisms between l-serine and O-phospho-l-serine with calcium hydroxyapatite and copper modified hydroxyapatite in relation with the acidity of aqueous medium

et al. 2018

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Motivated by the role of copper ions in biological processes the aim of this study was to elucidate the impact of copper ions bound to hydroxyapatite on L-serine (L-Ser) and O-phospho-L-serine (O-Ph-L-Ser) adsorption at different acidity of aqueous solutions. The adsorption phenomenon was studied by FTIR, UV, and AA spectroscopy, XRD and thermal analysis methods together with the evolved gases analysis taking into consideration the ionic state of the amino acids as well as the apatite surface state, which are tightly correlated with the solution pH. In acidic solution, the main process involves apatite dissolution releasing calcium and copper ions. At pH > 5 the complexation of amino acids with Ca or Cu ions is more important leading also to the release of cations. The ability of copper ions to form water soluble complexes with L-Ser and O-Ph-L-Ser leads to an important loss of these ions, while calcium release is very low at this pH. Therefore, the use of copper ions substituting calcium in the apatite structure to enhance the ability of amino acids adsorption on the apatite surface seems problematic even at pH > 5.

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“…Keratin is a polyampholyte with pI of 4.7-5.4 [66], so the charge deployed on it is pH-dependent and negative at physiological pH. The incoming phosphate group further enforces that negative charge, as its pK a2 = 5.78 [67], thus resulting in higher dye affinity to the hair and elevated Q values (Figs. 2, 3, 4B, 6B).…”

Section: Discussionmentioning

confidence: 99%

Enzymatic phosphorylation of hair keratin enhances fast adsorption of cationic moieties

Volkov

Cavaco-Paulo

2016

International Journal of Biological Macromolecules

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The current study describes the in vitro phosphorylation of a human hair keratin, using protein kinase for the first time. Phosphorylation of keratin was demonstrated by (31)P NMR (Nuclear Magnetic Resonance) and Diffuse Reflectance Infrared Fourier Transform (DRIFT) techniques. Phosphorylation induced a 2.5 fold increase of adsorption capacity in the first 10 min for cationic moiety like methylene blue (MB). Thorough description of MB adsorption process was performed by several isothermal models. Reconstructed fluorescent microscopy images depict distinct amounts of dye bound to the differently treated hair. The results of this work suggest that the enzymatic phosphorylation of keratins might have significant implications in hair shampooing and conditioning, where short application times of cationic components are of prime importance.

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Theoretical pKa prediction of O-phosphoserine in aqueous solution

Cited by 30 publications

References 42 publications

Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: A platform for the production of tuneable material

Phosphorylation of silk fibroins improves the cytocompatibility of silk fibroin derived materials: A platform for the production of tuneable material

Dependence of the interaction mechanisms between l-serine and O-phospho-l-serine with calcium hydroxyapatite and copper modified hydroxyapatite in relation with the acidity of aqueous medium

Enzymatic phosphorylation of hair keratin enhances fast adsorption of cationic moieties

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