Abstract
Lactoferrins are an iron-binding glycoprotein that have important protective roles in the mammalian body through their numerous functions, which include antimicrobial, antitumor, anti-inflammatory, immunomodulatory, and antioxidant activities. Among these, their antimicrobial activity has been the most studied, although the mechanism behind antimicrobial activities remains to be elucidated. Thirty years ago, the first lactoferrin-derived peptide was isolated and showed higher antimicrobial activity than the native lactoferrin lactoferricin. Since then, numerous studies have investigated the antimicrobial potencies of lactoferrins, lactoferricins, and other lactoferrin-derived peptides to better understand their antimicrobial activities at the molecular level. This review defines the current antibacterial, antiviral, antifungal, and antiparasitic activities of lactoferrins, lactoferricins, and lactoferrin-derived peptides. The primary focus is on their different mechanisms of activity against bacteria, viruses, fungi, and parasites. The role of their structure, amino-acid composition, conformation, charge, hydrophobicity, and other factors that affect their mechanisms of antimicrobial activity are also reviewed.
Highlights
Lactoferrins are iron-binding proteins that belong to the transferrin family
The term lactoferrinderived peptides is used to refer to peptides that are based on the lactoferrin molecule, with lactoferricin-derived peptides referring to peptides that are based on the lactoferricin sequence, which are shorter versions of the lactoferricin peptides
This review set out to clarify some aspects behind the mechanisms of lactoferrin and lactoferricin antimicrobial activities
Summary
Lactoferrins are iron-binding proteins that belong to the transferrin family. Since the first isolation of lactoferrins from both bovine [1] and human [2,3] milk in 1960, they have been the subject of intensive structural and functional studies, especially because of their numerous functions, properties, and applications in the food and pharmaceutical industries. Lactoferrins are produced by the epithelial cells of different body organs [4], and as a consequence, they are found in numerous exocrine secretions, including the colostrum, milk, tears, nasal and bronchial secretions, saliva, bile and pancreatic secretions (and in gastric and intestinal fluids), urine, and seminal and vaginal fluids [5]. The primary amino-acid sequences of lactoferrins from different mammalian species have been reported, including those for human [15,17], cow [18,19], goat [20,21], sheep [13], camel [22], buffalo [23], horse [24], pig [25], and mouse [26]. The term lactoferrinderived peptides is used to refer to peptides that are based on the lactoferrin molecule, with lactoferricin-derived peptides referring to peptides that are based on the lactoferricin sequence, which are shorter versions of the lactoferricin peptides
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