Stability and angiotensin converting enzyme inhibitory activity of peptide RVPSL-loaded graphene oxide


Citation

Zhang M., . and Guo H., . and Li J., . and Yu Z., . and Zhao W., . and Liu J., . Stability and angiotensin converting enzyme inhibitory activity of peptide RVPSL-loaded graphene oxide. pp. 173-180. ISSN 22317546

Abstract

Previous work has demonstrated that the angiotensin converting enzyme (ACE) inhibitory peptide RVPSL is very unstable and loses its ACE inhibitory activity in the gastrointestinal tract. Thus graphene oxide (GO) was used to improve the stability of RVPSL in the present work. The structure and morphology of RVPSL-GO were characterised using Fourier transform-infrared spectroscopy X-ray photoelectron spectroscopy scanning electron microscopy and atomic force microscopy. Moreover the cytotoxicity of RVPSL-GO was examined using HepG2 cells. RVPSL was successfully covalently bonded to GO and the RVPSL-loading capacities of RVPSL-GO were calculated to be 1.05 mg RVPSL/mg GO and the loading efficiency value was 95.02. The results showed that GO enhanced RVPSL ACE activity (at 0.026 mg/mL) from 26.47 to 39.70. This may have caused a higher local concentration of RVPSL in the solution after GO was modified. Moreover the stability of RVPSL was improved with protection from GO. The ACE inhibition rate of RVPSL-GO was 49.08 while RVPSL was completely degraded after 2 h in simulated gastrointestinal digestion. In addition RVPSL-GO displayed high viability for HepG2 cells with no significant cytotoxicity.


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Abstract

Previous work has demonstrated that the angiotensin converting enzyme (ACE) inhibitory peptide RVPSL is very unstable and loses its ACE inhibitory activity in the gastrointestinal tract. Thus graphene oxide (GO) was used to improve the stability of RVPSL in the present work. The structure and morphology of RVPSL-GO were characterised using Fourier transform-infrared spectroscopy X-ray photoelectron spectroscopy scanning electron microscopy and atomic force microscopy. Moreover the cytotoxicity of RVPSL-GO was examined using HepG2 cells. RVPSL was successfully covalently bonded to GO and the RVPSL-loading capacities of RVPSL-GO were calculated to be 1.05 mg RVPSL/mg GO and the loading efficiency value was 95.02. The results showed that GO enhanced RVPSL ACE activity (at 0.026 mg/mL) from 26.47 to 39.70. This may have caused a higher local concentration of RVPSL in the solution after GO was modified. Moreover the stability of RVPSL was improved with protection from GO. The ACE inhibition rate of RVPSL-GO was 49.08 while RVPSL was completely degraded after 2 h in simulated gastrointestinal digestion. In addition RVPSL-GO displayed high viability for HepG2 cells with no significant cytotoxicity.

Additional Metadata

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Item Type: Article
AGROVOC Term: Peptides
AGROVOC Term: Angiotensin
AGROVOC Term: Enzyme inhibitors
AGROVOC Term: X ray spectroscopy
AGROVOC Term: Scanning microscopy
AGROVOC Term: Cytotoxicity
AGROVOC Term: Stability
Depositing User: Mr. AFANDI ABDUL MALEK
Last Modified: 24 Apr 2025 00:55
URI: http://webagris.upm.edu.my/id/eprint/9655

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