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The Nutraceutical Properties of Ovotransferrin and Its Potential Utilization as a Functional Food.

Giansanti F, Leboffe L, Angelucci F, Antonini G - Nutrients (2015)

Bottom Line: Ovotransferrin or conalbumin belong to the transferrin protein family and is endowed with both iron-transfer and protective activities.In addition to its well-known antibacterial properties, ovotransferrin displays other protective roles similar to those already ascertained for the homologous mammalian lactoferrin.These additional functions, in many cases not directly related to iron binding, are also displayed by the peptides derived from partial hydrolysis of ovotransferrin, suggesting a direct relationship between egg consumption and human health.

View Article: PubMed Central - PubMed

Affiliation: Department of Health, Life and Environmental Sciences, University of L'Aquila, L'Aquila I-67100, Italy. francesco.giansanti@cc.univaq.it.

ABSTRACT
Ovotransferrin or conalbumin belong to the transferrin protein family and is endowed with both iron-transfer and protective activities. In addition to its well-known antibacterial properties, ovotransferrin displays other protective roles similar to those already ascertained for the homologous mammalian lactoferrin. These additional functions, in many cases not directly related to iron binding, are also displayed by the peptides derived from partial hydrolysis of ovotransferrin, suggesting a direct relationship between egg consumption and human health.

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Related in: MedlinePlus

(A) Ribbon representation and the solvent-accessible surface (in transparency) of holo-Otrf (PDB ID:1OVT) [16]. N1, N2 and C1, C2 indicate the subdomains of each lobe. (B) The N-lobe iron binding site of hen’s ovotransferrin (PDB ID:1OVT). The amino acids involved in iron binding are shown in sticks. H-bonds are displayed by purple broken lines. Both in (A) and (B), the iron is indicated as a yellow sphere. (C) Schematic ribbon representation of the OTAP-92 peptide. The three disulfide linkages are represented in yellow, while the hydrophobic residues are highlighted in blue. The peptide is shown with the same conformation displayed in the intact protein. Molecular graphic images were produced using the UCSF chimera package [20].
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nutrients-07-05453-f001: (A) Ribbon representation and the solvent-accessible surface (in transparency) of holo-Otrf (PDB ID:1OVT) [16]. N1, N2 and C1, C2 indicate the subdomains of each lobe. (B) The N-lobe iron binding site of hen’s ovotransferrin (PDB ID:1OVT). The amino acids involved in iron binding are shown in sticks. H-bonds are displayed by purple broken lines. Both in (A) and (B), the iron is indicated as a yellow sphere. (C) Schematic ribbon representation of the OTAP-92 peptide. The three disulfide linkages are represented in yellow, while the hydrophobic residues are highlighted in blue. The peptide is shown with the same conformation displayed in the intact protein. Molecular graphic images were produced using the UCSF chimera package [20].

Mentions: Like the mammalian transferrins, the single chain of Otrf consists of two globular lobes (N- and C-lobes), interconnected by a α-helix of nine amino acidic residues (residues 333–341) that can be released by tryptic digestion. Each lobe contains an iron binding site and is divided in two domains, (domains N1 and N2 in the N-lobe and domains C1 and C2 in the C-lobe, respectively; Figure 1A) [16,17,18].


The Nutraceutical Properties of Ovotransferrin and Its Potential Utilization as a Functional Food.

Giansanti F, Leboffe L, Angelucci F, Antonini G - Nutrients (2015)

(A) Ribbon representation and the solvent-accessible surface (in transparency) of holo-Otrf (PDB ID:1OVT) [16]. N1, N2 and C1, C2 indicate the subdomains of each lobe. (B) The N-lobe iron binding site of hen’s ovotransferrin (PDB ID:1OVT). The amino acids involved in iron binding are shown in sticks. H-bonds are displayed by purple broken lines. Both in (A) and (B), the iron is indicated as a yellow sphere. (C) Schematic ribbon representation of the OTAP-92 peptide. The three disulfide linkages are represented in yellow, while the hydrophobic residues are highlighted in blue. The peptide is shown with the same conformation displayed in the intact protein. Molecular graphic images were produced using the UCSF chimera package [20].
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4663581&req=5

nutrients-07-05453-f001: (A) Ribbon representation and the solvent-accessible surface (in transparency) of holo-Otrf (PDB ID:1OVT) [16]. N1, N2 and C1, C2 indicate the subdomains of each lobe. (B) The N-lobe iron binding site of hen’s ovotransferrin (PDB ID:1OVT). The amino acids involved in iron binding are shown in sticks. H-bonds are displayed by purple broken lines. Both in (A) and (B), the iron is indicated as a yellow sphere. (C) Schematic ribbon representation of the OTAP-92 peptide. The three disulfide linkages are represented in yellow, while the hydrophobic residues are highlighted in blue. The peptide is shown with the same conformation displayed in the intact protein. Molecular graphic images were produced using the UCSF chimera package [20].
Mentions: Like the mammalian transferrins, the single chain of Otrf consists of two globular lobes (N- and C-lobes), interconnected by a α-helix of nine amino acidic residues (residues 333–341) that can be released by tryptic digestion. Each lobe contains an iron binding site and is divided in two domains, (domains N1 and N2 in the N-lobe and domains C1 and C2 in the C-lobe, respectively; Figure 1A) [16,17,18].

Bottom Line: Ovotransferrin or conalbumin belong to the transferrin protein family and is endowed with both iron-transfer and protective activities.In addition to its well-known antibacterial properties, ovotransferrin displays other protective roles similar to those already ascertained for the homologous mammalian lactoferrin.These additional functions, in many cases not directly related to iron binding, are also displayed by the peptides derived from partial hydrolysis of ovotransferrin, suggesting a direct relationship between egg consumption and human health.

View Article: PubMed Central - PubMed

Affiliation: Department of Health, Life and Environmental Sciences, University of L'Aquila, L'Aquila I-67100, Italy. francesco.giansanti@cc.univaq.it.

ABSTRACT
Ovotransferrin or conalbumin belong to the transferrin protein family and is endowed with both iron-transfer and protective activities. In addition to its well-known antibacterial properties, ovotransferrin displays other protective roles similar to those already ascertained for the homologous mammalian lactoferrin. These additional functions, in many cases not directly related to iron binding, are also displayed by the peptides derived from partial hydrolysis of ovotransferrin, suggesting a direct relationship between egg consumption and human health.

Show MeSH
Related in: MedlinePlus