shahsavari, abbas and Gheibi, Nematollah and Goodarzvand Chegini, Koorosh (2016) Modification of the structure of natural and modified forms calprotectin subunits expressed S100A8/ S100A9. Masters thesis, Qazvin university of medical science.
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Abstract
Calprotectin is member of the S-100 protein family with a wide plethora of intra-and extracellular functions. Anticancer activities, antimicrobial effects and being a qualified disease marker are among the compelling features of this protein to be used as a pharmaceutical agent. However, there are several impediments to applications of protein pharmaceuticals including: proteolytic degradation, short circulating half-life, low solubility and immunogenicity. PEG is a common bioconjugation polymer capable of overcoming these drawbacks. Two hundred μl of S100A8/9+Ca complex (1.9mg/l), was dissolved in 100ml of 0.1M sodium tetraborate at 3 different pH (6.5, 7.2 and 9.2). This solution and activated mPEG in different ratio concentration (0.01mM 0.025mM, 0.001mM) were mixed at 4˚C and room temperature. After 1h uncoupled mPEG was removed by dialysis using PBS dialysis buffer (Nacl 25mM, NaH2PO4 100mM, pH=7.2) for 18 h according to. Recombinant expression and purification of calprotectin along with its PEGylation would result in enhanced pharmacodynamic and pharmacokinetic properties. Our florescence spectroscopy and far UV-OD results indicate that PEGylation altered the physical and structural properties of the calprotectin to become in a more stable and functionally active state. Due to enhanced pharmacodynamic and pharmacokinetic properties of the calprotectin via PEGylation, this study would pave the way for better in vitro and in vivo validations of calprotectin applications in medical practice.
| Item Type: | Thesis (Masters) |
|---|---|
| Subjects: | R Medicine > RP Paramedical > RP105 Biotechnology R Medicine > RS Pharmacy and materia medica |
| Divisions: | University Thesis > Faculty of Paramedicals |
| Depositing User: | Paramedicals School Students |
| Date Deposited: | 13 Jan 2016 08:31 |
| Last Modified: | 14 Jan 2017 08:12 |
| URI: | http://eprints.qums.ac.ir/id/eprint/3550 |
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