ArticleAntimicrobial agents and chemotherapy2005
Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent.
Article in Antimicrobial agents and chemotherapy, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- Lactoferrin-Derived Peptides in Cancer Therapy: Structural Features, Mechanistic Insights and Clinical Translation Prospects.International journal of molecular sciences · 2026Review
- Human and Marine Host Defense Peptides for Healthy Skin.Marine drugs · 2026Review
- Article
- Addressing the silent threat: managing invasiveFrontiers in pediatrics · 2025Review
- Lactoferrin Binds through Its N-Terminus to the Receptor-Binding Domain of the SARS-CoV-2 Spike Protein.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Lactoferrins in Their Interactions with Molecular Targets: A Structure-Based Overview.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Time to Kill and Time to Heal: The Multifaceted Role of Lactoferrin and Lactoferricin in Host Defense.Pharmaceutics · 2023Review
- Molecular characterization of the PhiKo endolysin fromFrontiers in microbiology · 2023Article
- High expression of antimicrobial peptides cathelicidin-BF inFrontiers in microbiology · 2023Article
- Mammals' humoral immune proteins and peptides targeting the bacterial envelope: from natural protection to therapeutic applications against multidrug-resistant Gram-negatives.Biological reviews of the Cambridge Philosophical Society · 2022Review
- A review on antimicrobial peptides databases and the computational tools.Database : the journal of biological databases and curation · 2022Review
- Blockade of TMPRSS2-mediated priming of SARS-CoV-2 by lactoferricin.Frontiers in immunology · 2022Article
- Diverse Mechanisms of Antimicrobial Activities of Lactoferrins, Lactoferricins, and Other Lactoferrin-Derived Peptides.International journal of molecular sciences · 2021Review
- Article
- Antimicrobial Peptides and Proteins: From Nature's Reservoir to the Laboratory and Beyond.Frontiers in chemistry · 2021Review
- Lactoferrin-Derived Peptide Lactofungin Is Potently Synergistic with Amphotericin B.Antimicrobial agents and chemotherapy · 2020Article
- Design, Engineering and Discovery of Novel α-Helical and β-Boomerang Antimicrobial Peptides against Drug Resistant Bacteria.International journal of molecular sciences · 2020Review
- Lactoferrin-Hexon Interactions Mediate CAR-Independent Adenovirus Infection of Human Respiratory Cells.Journal of virology · 2020Article
- The Impact of Lactoferrin on the Growth of Intestinal Inhabitant Bacteria.International journal of molecular sciences · 2019Review
- Antioxidative Peptides from Proteolytic Hydrolysates of False Abalone (Marine drugs · 2019Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactoferricins are highly basic bioactive peptides that are released in the stomach through proteolytic cleavage of various lactoferrin proteins. Here we have determined the solution structure of human lactoferricin (LfcinH) by conventional two-dimensional nuclear magnetic resonance methods in both aqueous solution and a membrane mimetic solvent. Unlike the 25-residue bovine lactoferricin (LfcinB), which adopts a somewhat distorted antiparallel beta sheet, the longer LfcinH peptide shows a helical content from Gln14 to Lys29 in the membrane mimetic solvent but a nonexistent beta-sheet character in either the N- or C-terminal regions of the peptide. The helical characteristic of the LfcinH peptide resembles the conformation that this region adopts in the crystal structure of the intact protein. The LfcinH structure determined in aqueous solution displays a nascent helix in the form of a coiled conformation in the region from Gln14 to Lys29. Numerous hydrophobic interactions create the basis for the better-defined overall structure observed in the membrane mimetic solvent. The 49-residue LfcinH peptide isolated for these studies was found to be slightly longer than previously reported peptide preparations and was found to have an intact peptide bond between residues Ala11 and Val12. The distinct solution structures of LfcinH and LfcinB represent a novel difference in the physical properties of these two peptides, which contributes to their unique physiological activities.
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