ArticleNutrients2024
Effects of Forming Lactoferrin-Milk Protein Complexes on Lactoferrin Functionality and Intestinal Development in Infancy.
Article in Nutrients, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- From homeostasis to dysregulation: human milk, microbial metabolites, and the preterm intestinal microenvironment in necrotizing enterocolitis.Translational pediatrics · 2026Review
- From dairy by-product to cell feed: milk whey for serum-free media and scaffold development in cell-based food production.NPJ science of food · 2026Review
- From Cheese Whey to Functional Ingredients: Upcycling Whey Proteins for Cardiovascular and Immunomodulatory Health-Evidence Mapping and Perspectives from Portugal.Foods (Basel, Switzerland) · 2026Review
- Lactoferrin as a Candidate Multifunctional Therapeutic in Synucleinopathies.Brain sciences · 2025Review
- Impact of bovine lactoferrin supplementation and reduced iron in formula on infant oral microbiome: a randomized controlled trial.Journal of oral microbiology · 2025Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
BACKGROUND/
objectivesLactoferrin (Lf) is an iron-binding glycoprotein with multiple bioactivities, including promotion of cell proliferation and differentiation, immunomodulation, and antimicrobial activity. Lf, a basic glycoprotein, can bind to α-lactalbumin (α-Lac), an acidic whey protein. The current study aimed to evaluate whether Lf forms protein complexes with α-Lac and proteins/peptides from whey protein hydrolysate (WPH) and nonfat bovine milk powder (MP) and whether forming protein complexes influences resistance to gastrointestinal digestion and affects the bioactivities of Lf in human intestinal epithelial cells (HIECs and differentiated Caco-2 cells).
methodsLf was blended with α-Lac, WPH, or MP. Assays were conducted to evaluate the bioactivities of proteins (Lf, α-Lac, WPH, or MP) and Lf-protein blends on HIECs and Caco-2 cells.
results(1) Lf forms complexes with α-Lac and proteins/peptides from WPH and MP; (2) compared with Lf alone, complexed Lf shows greater resistance to in vitro digestion; (3) forming protein complexes does not affect Lf's binding to the Lf receptor or its uptake by HIECs; and (4) forming protein complexes does not impact Lf's bioactivities, including the promotion of cell proliferation and differentiation, reduction of cell permeability by upregulating tight-junction proteins, immune modulation through the regulation of IL-18, inhibition of enteropathogenic
conclusionsLf forms complexes with α-Lac and other milk proteins/peptides from WPH and MP in protein blends, and forming complexes does not affect the functionalities of Lf.
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Registered trials
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