| Autor: |
Dai LIN, Guanzhen GAO, Jianwu ZHOU, Lijing KE, Pingfan RAO |
| Jazyk: |
čínština |
| Rok vydání: |
2023 |
| Předmět: |
|
| Zdroj: |
Shipin gongye ke-ji, Vol 44, Iss 9, Pp 20-26 (2023) |
| Druh dokumentu: |
article |
| ISSN: |
1002-0306 |
| DOI: |
10.13386/j.issn1002-0306.2022100193 |
| Popis: |
Objective: To purify and characterize a water-soluble protein from Pueraria lobata and to fabricate its nanoparticles by heating-induced assembly. Methods: Pueraria lobata protein was purified by anion exchange chromatography High Q, and its molecular weight and amino acid sequence were determined by SDS-PAGE and N-terminal sequencing. The particle size, optical dispersion intensity and Zeta potential of protein nanoparticles were measured by laser-scattering particle analyzer. The drug loading efficiency of the nanocarrier was determined by chromatography. Results: A major water-soluble protein, named PP, was purified from Pueraria lobata and sequenced with a N-terminal amino acid sequence of DFVYDMCGNVLNGGTYYIL. PP was identified as a novel trypsin inhibitor by NCBI database searching and rypsin inhibitory assay. PP was also well-stabilized in the pH2~10 and 20~50 °C ranges. After heating PP solution (0.1 mg/mL, pH6.0) for 60 minutes at 100 ℃, homogenous nanoparticles (PP-NPs) were harvested. These PP-NPs had a particle size of 172.78 nm and a Zeta potential of −25.40 mV. The puerarin and berberine were effectively loaded onto PP-NPs, with loading efficiency of 33.83% and 24.61%, respectively. Conclusion: The major water-soluble Pueraria lobata protein PP can be fabricated into protein nanoparticles by heating-induced assembly, indicating a potential as drug carriers. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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