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Phycobiliproteins from Arthrospira Platensis (Spirulina): A New Source of Peptides with Dipeptidyl Peptidase-IV Inhibitory Activity.
Nutrients. 2020 Mar 18; 12(3)N

Abstract

Arthrospira platensis (spirulina) is a cyanobacterium, which contains mainly two phycobiliproteins (PBP), i.e., C-phycocyanin (C-PC) and allophycocyanin (APC). In this study, PBP were hydrolyzed using trypsin, and the composition of the hydrolysate was characterized by HPLC-ESI-MS/MS. Furthermore, the potential anti-diabetic activity was assessed by using either biochemical or cellular techniques. Findings suggest that PBP peptides inhibit DPP-IV activity in vitro with a dose-response trend and an IC50 value falling in the range between 0.5 and 1.0 mg/mL. A lower inhibition of the DPP-IV activity expressed by Caco-2 cells was observed, which was explained by a secondary metabolic degradation exerted by the same cells.

Authors+Show Affiliations

Department of Pharmaceutical Sciences, University of Milan, 20133 Milan, Italy.Department of Pharmaceutical Sciences, University of Milan, 20133 Milan, Italy.Department of Pharmaceutical Sciences, University of Milan, 20133 Milan, Italy.Department of Pharmaceutical Sciences, University of Milan, 20133 Milan, Italy.Department of Pharmaceutical Sciences, University of Milan, 20133 Milan, Italy.Department of Pharmaceutical Sciences, University of Milan, 20133 Milan, Italy.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32197331

Citation

Li, Yuchen, et al. "Phycobiliproteins From Arthrospira Platensis (Spirulina): a New Source of Peptides With Dipeptidyl Peptidase-IV Inhibitory Activity." Nutrients, vol. 12, no. 3, 2020.
Li Y, Aiello G, Bollati C, et al. Phycobiliproteins from Arthrospira Platensis (Spirulina): A New Source of Peptides with Dipeptidyl Peptidase-IV Inhibitory Activity. Nutrients. 2020;12(3).
Li, Y., Aiello, G., Bollati, C., Bartolomei, M., Arnoldi, A., & Lammi, C. (2020). Phycobiliproteins from Arthrospira Platensis (Spirulina): A New Source of Peptides with Dipeptidyl Peptidase-IV Inhibitory Activity. Nutrients, 12(3). https://doi.org/10.3390/nu12030794
Li Y, et al. Phycobiliproteins From Arthrospira Platensis (Spirulina): a New Source of Peptides With Dipeptidyl Peptidase-IV Inhibitory Activity. Nutrients. 2020 Mar 18;12(3) PubMed PMID: 32197331.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Phycobiliproteins from Arthrospira Platensis (Spirulina): A New Source of Peptides with Dipeptidyl Peptidase-IV Inhibitory Activity. AU - Li,Yuchen, AU - Aiello,Gilda, AU - Bollati,Carlotta, AU - Bartolomei,Martina, AU - Arnoldi,Anna, AU - Lammi,Carmen, Y1 - 2020/03/18/ PY - 2020/02/27/received PY - 2020/03/12/revised PY - 2020/03/16/accepted PY - 2020/3/22/entrez PY - 2020/3/22/pubmed PY - 2021/1/7/medline KW - C-Phycocyanin KW - DPP-IV KW - LC-MS/MS KW - Spirulina platensis KW - allophycocyanin KW - bioactive peptides JF - Nutrients JO - Nutrients VL - 12 IS - 3 N2 - Arthrospira platensis (spirulina) is a cyanobacterium, which contains mainly two phycobiliproteins (PBP), i.e., C-phycocyanin (C-PC) and allophycocyanin (APC). In this study, PBP were hydrolyzed using trypsin, and the composition of the hydrolysate was characterized by HPLC-ESI-MS/MS. Furthermore, the potential anti-diabetic activity was assessed by using either biochemical or cellular techniques. Findings suggest that PBP peptides inhibit DPP-IV activity in vitro with a dose-response trend and an IC50 value falling in the range between 0.5 and 1.0 mg/mL. A lower inhibition of the DPP-IV activity expressed by Caco-2 cells was observed, which was explained by a secondary metabolic degradation exerted by the same cells. SN - 2072-6643 UR - https://www.unboundmedicine.com/medline/citation/32197331/Phycobiliproteins_from_Arthrospira_Platensis__Spirulina_:_A_New_Source_of_Peptides_with_Dipeptidyl_Peptidase_IV_Inhibitory_Activity_ DB - PRIME DP - Unbound Medicine ER -