Structure–activity relationships of αs-casein peptides with multifunctional biological activities
Abstract
Multifunctional bioactive peptides have a wider role in modulating physiological functions and possess multiple biological activities. Peptides from bovine milk with sequences QKALNEINQF [p10] and TKKTKLTEEEKNRL [p14] from α-S2 casein f (79-88) and α-S2 casein f (148-161) were identified to be having multifunctional biological activities and were synthesized. These synthesized peptides show various biological activities like angiotensin-converting enzyme inhibition, prolyl endopeptidase inhibition, antioxidant, and antimicrobial activities. The mode of antimicrobial mechanism was studied and p10 shows depolarization of cell membrane, whereas p14 was found to display DNA-binding activity. Structural studies envisaged backbone flexibility, for differences in their mode of action. Peptide structure function studies were correlated to understand their multifunctional biological activity.
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Peptide fragment αs1-CN (f148-161) produced by cleavage at Phe-Thr is a bioactive peptide with angiotensin-converting enzyme (ACE) inhibitory activity.
“Likewise, peptide fragment α -CN (f148-161) produced by cleavage at Phe -Thr is a bioactive peptide (Table 2) with angiotensinconverting enzyme (ACE) inhibitory activity, (Sistla, 2013).”
From Proteolysis in Irish farmhouse Camembert cheese during ripening (2020) · cites this paper as Sistla, 2013
Cites
Bioactive milk peptides: a prospectus.
Clare, D. A., & Swaisgood, H. E. (2000) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(00)74983-6 · Cited by 718 · see citing works
Cell-permeable, mitochondrial-targeted, peptide antioxidants
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Isolation and characterisation of a novel antibacterial peptide from bovine αS1-casein
McCann, K. B., Shiell, B. J., Michalski, W. P., Lee, A., Wan, J., Roginski, H., & Coventry, M. J. (2006) · International Dairy Journal · doi:10.1016/j.idairyj.2005.05.005 · Cited by 133 · see citing works
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Proteolysis in Irish farmhouse Camembert cheese during ripening
Mane, A., & McSweeney, P. L. H. (2020) · Journal of Food Biochemistry · doi:10.1111/jfbc.13101 · Cited by 35 · see citing works
“(ACE) Milk 28–34 Sun and Jenssen (2012) αs1-CN HIQKEDVPSER Antioxidant Milk 80–90 Baum et al. (2013) αs2-CN TKKTKLTEEEKNRL ACE Milk 148–161 Sistla (2013) β-CN DKIHPF ACE Cheddar, Manchego 47–52 Gómez-Ruiz, Taborda, Amigo, Recio and Ramos (2006) β-CN KVLPVPQ Antihypersensitive Milk 169–175 Park…”
Background
- Authors
- Sistla, S.
- Affiliations
- Central Food Technological Research Institute (IN)
- Corresponding author
- Sistla, Srinivas
- ORCID
- Sistla, Srinivas
- Venue
- Molecular and Cellular Biochemistry
- Published
- 2013-08-21
- Volume
- 384
- Issue
- 1-2
- Pages
- 29-38
- ISSN
- 0300-8177 (ISSN-L)
- 1573-4919
- OpenAlex
- W2461121283
- Cited by
- 28
- References
- 4
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 2 · 2023: 2 · 2022: 2 · 2021: 1 · 2020: 3 · 2019: 2 · 2018: 3 · 2017: 4 · 2016: 3 · 2015: 1
- FWCI
- 0.60
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Molecular and Cellular Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Keywords
- cow's milk, structure-activity relationship, angiotensin-converting enzyme inhibition, prolyl endopeptidase inhibition, antioxidant activity, antimicrobial activity, membrane depolarization, DNA-binding activity, peptide synthesis, backbone flexibility
- MeSH terms
- Prolyl Oligopeptidases, Angiotensin-Converting Enzyme Inhibitors, Animals, Antioxidants, Bacillus cereus, Caseins, DNA-Binding Proteins, Listeria monocytogenes, Microbial Sensitivity Tests, Milk, Serine Endopeptidases, Staphylococcus aureus, Structure-Activity Relationship, Helicobacter pylori, Protein Structure, Secondary, Antimicrobial Cationic Peptides
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