Cited by 83Protein Hydrolysis and Bioactive PeptidesSeaweed-derived Bioactive CompoundsAdvanced Proteomics Techniques and Applications

Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina

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Minic, Simeon L., Stanic-Vucinic, Dragana, Mihailovic, Jelena, Krstic, Maja, Nikolic, Milan R., Cirkovic Velickovic, Tanja·2016·Journal of Proteomics

Abstract

C-phycocyanin, the major protein of cyanobacteria Spirulina, possesses significant antioxidant, anti-cancer, anti-inflammatory and immunomodulatory effects, ascribed to covalently attached linear tetrapyrrole chromophore phycocyanobilin. There are no literature data about structure and biological activities of released peptides with bound chromophore in C-phycocyanin digest. This study aims to identify chromopeptides obtained after pepsin digestion of C-phycocyanin and to examine their bioactivities. C-phycocyanin is rapidly digested by pepsin in simulated gastric fluid. The structure of released chromopeptides was analyzed by high resolution tandem mass spectrometry and peptides varying in size from 2 to 13 amino acid residues were identified in both subunits of C-phycocyanin. Following separation by HPLC, chromopeptides were analyzed for potential bioactivities. It was shown that all five chromopeptide fractions have significant antioxidant and metal-chelating activities and show cytotoxic effect on human cervical adenocarcinoma and epithelial colonic cancer cell lines. In addition, chromopeptides protect human erythrocytes from free radical-induced hemolysis in antioxidative capacity-dependant manner. There was a positive correlation between antioxidative potency and other biological activities of chromopeptides. Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin whose activity is mostly related to the antioxidative potency provided by chromophore.

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Crossref · 10.1016/j.jprot.2016.03.043

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Authors
Minic, S. L., Stanic-Vucinic, D., Mihailovic, J., Krstic, M., Nikolic, M. R., & Cirkovic Velickovic, T.
Affiliations
University of Belgrade (RS)
Venue
Journal of Proteomics
Publisher
Elsevier BV
Published
2016-09
Volume
147
Pages
132-139
ISSN
1874-3919 (ISSN-L)
OpenAlex
W2342272883
Cited by
83
References
58
Citations by year
2026: 16 · 2025: 8 · 2024: 9 · 2023: 8 · 2022: 10 · 2021: 11 · 2020: 6 · 2019: 4 · 2018: 8 · 2017: 2 · 2016: 1
FWCI
2.60
Type
journal article
Language
en
Open access
Locations
  • Journal of Proteomics (publishedVersion)
  • PubMed (publishedVersion)
  • Ghent University Academic Bibliography (Ghent University) (submittedVersion)
  • Cherry (Univesrity of Belgrade, Faculty of Chemistry) (submittedVersion)
  • Cherry (Univesrity of Belgrade, Faculty of Chemistry) (submittedVersion, cc-by-nc-nd)
Funders
  • Seventh Framework Programme (256716)
  • Ministarstvo Prosvete, Nauke i Tehnološkog Razvoja (172024)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
  • Life Sciences › Agricultural and Biological Sciences › Aquatic Science › Seaweed-derived Bioactive Compounds
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Keywords
C-phycocyanin, pepsin digestion, chromopeptides, phycocyanobilin, antioxidant activity, metal chelating activity, cytotoxicity, colon cancer cells, erythrocyte hemolysis, free radical protection, Spirulina, cyanobacteria, simulated gastric fluid
MeSH terms
Antioxidants, Cells, Cultured, Uterine Cervical Neoplasms, Colonic Neoplasms, Color, Erythrocytes, Female, Hemolysis, Humans, Pepsin A, Peptides, Phycocyanin, Cell Line, Tumor, Spirulina

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