Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (675 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
The major protein constituents of milk are caseins and whey proteins such as lactalbumin and lactoglobulins. immunoglobulins occur in high concentrations in colostrum and in relatively lower concentrations in milk. (Singleton and Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed, p554)
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Milk Protein; Protein, Milk; Proteins, Milk.
Where it fits in the MeSH classification
- Broader topics
- Milk; Animal Proteins, Dietary
- Narrower topics
- Whey Proteins; Caseins
Related concepts
- Caseins
- Lactalbumin
- Lactoglobulins
- Immunoglobulins
- Colostrum
Research landscape
PubMed indexes 45,037 records tagged with the MeSH heading “Milk Proteins” (counts retrieved 2026-10-31). 7,730 of them (17.2%) were published from 2020 onward, and the busiest period so far is through 1999 with 17,402 records.
Reviews account for 2,718 records (6.0%) and meta-analyses for 201. Randomized controlled trials number 1,697 (3.8%) as a share of all records on the topic.
Show the data
| Period | Records |
|---|---|
| through 1999 | 17,402 |
| 2000-2009 | 9,070 |
| 2010-2019 | 10,835 |
| 2020 onward | 7,730 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 2,718 | 6.0% |
| Meta-analyses | 201 | 0.4% |
| Randomized controlled trials | 1,697 | 3.8% |
Method: PubMed query "Milk Proteins"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-31.
Reading the evidence in anatomy and physiology
Anatomy describes how body structures are built and physiology describes how they normally work, so most findings here are descriptive or mechanistic rather than evidence about treatment. Much of what is known comes from dissection, imaging, tissue studies and experiments in animals, and measurements in healthy volunteers can differ from those in people with disease or at different ages. Normal ranges vary between individuals and populations. Check whether a result was measured in people or in another species, the age and health of the participants, and the method used.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
Lactoferrin: Properties and Potential Uses in the Food Industry [1]
Abstract reading summary — source excerpts
- Opening excerpt
- Lactoferrin (LF) is an 80 kDa glycoprotein that contains approximately 700 amino acids and is a member of the transferrin family.
- Closing excerpt
- This review discusses the attributes and safety of LF, particularly its exploitation in the food industry.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (217 words)
Lactoferrin (LF) is an 80 kDa glycoprotein that contains approximately 700 amino acids and is a member of the transferrin family. The essential properties of LF, including antimicrobial, antiviral, anticancer, anti-inflammatory, antioxidant, and probiotic effects, have been studied for decades. The iron chelation activity of LF is significantly associated with its antimicrobial, anti-inflammatory, and antioxidant properties. Owing to its probiotic and prebiotic activity, LF also facilitates the growth of beneficial microorganisms and iron-defense immediate-effect properties on pathogens. Additionally, the ability to regulate cell signaling pathways and immune responses makes LF a prominent modulatory protein. These diverse characteristics of LF have gained interest in its therapeutic potential. Studies have suggested that LF could serve as an alternative source to antibiotics in severe infections and illnesses. LF has also gained interest in the food industry for its potential as an additive to fortify products such as yogurt, infant formula, and meat derivatives while also improving the shelf life of foods and providing antimicrobial and antioxidant activity. Prior to using LF in the food industry, the safety and toxicity of food processing are necessary to be investigated. These safety investigations are crucial for addressing potential harm or side effects and ensuring a healthy lifestyle. This review discusses the attributes and safety of LF, particularly its exploitation in the food industry.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 40003872 · DOI · PMC11855648
Construction of nanodelivery system based on the interaction mechanism between ultrasound-treated soybean whey protein and quercetin: structure, physicochemical stability and bioaccessibility [2]
Abstract reading summary — source excerpts
- Opening excerpt
- In this study, soybean whey protein (SWP) nanodelivery system was constructed through ultrasound treatment and quercetin (Que) modification.
- Closing excerpt
- This study highlights the potential of ultrasound-modified SWP nanoparticles for effective nutrient delivery.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (145 words)
In this study, soybean whey protein (SWP) nanodelivery system was constructed through ultrasound treatment and quercetin (Que) modification. The effect of ultrasound power on the interaction mode between SWP and Que, and the formation and stability of SWP-Que nanodelivery system were investigated. Optimal ultrasound treatment (300-500 W) produced SWP-Que nanoparticles with smaller particle size, higher ζ-potential values, and more uniform dispersion. Fluorescence spectroscopy and FTIR analyses revealed that SWP primarily binds to Que through hydrophobic interactions. Ultrasound treatment induced the unfolding of the SWP structure, thereby increasing its binding affinity to Que. After 400 W sonication, the encapsulation efficiency can reach 95.63 ± 0.60 %. The SWP-Que nanoparticles protected Que from degradation under environmental stresses (heat, UV, and storage) and improved its bioaccessibility during digestion as the ultrasonic power of 400 W. This study highlights the potential of ultrasound-modified SWP nanoparticles for effective nutrient delivery.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 39671813 · DOI · PMC11700283
Continuous Protein Sensing Using Fast-Dissociating Antibody Fragments in Competition-Based Biosensing by Particle Motion [3]
Abstract reading summary — source excerpts
- Opening excerpt
- Sensing technologies for the continuous monitoring of protein concentrations are important for understanding time-dependent behaviors of biological systems and for controlling bioprocesses.
- Closing excerpt
- This work demonstrates how continuous protein sensing can be realized using fast-dissociating antibodies in a competitive sensor format.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (141 words)
Sensing technologies for the continuous monitoring of protein concentrations are important for understanding time-dependent behaviors of biological systems and for controlling bioprocesses. We present a continuous sensing methodology based on tethered particle motion (t-BPM) that utilizes fast-dissociating antibody fragments (Fabs) for continuous protein monitoring. A competition-based t-BPM sensor was developed and characterized utilizing custom-made Fabs. The sensing concept was demonstrated for lactoferrin, an 80 kDa iron-binding glycoprotein that is part of the innate immune response. Thirteen Fabs were compared using free particle motion sensing as well as surface plasmon resonance, of which six Fabs showed rapid association and dissociation. The integration of the Fabs into the t-BPM sensor enabled nanomolar lactoferrin detection in both buffer solutions and milk matrices over tens of hours. This work demonstrates how continuous protein sensing can be realized using fast-dissociating antibodies in a competitive sensor format.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 40126441 · DOI · PMC12038830
Lactoferrin blocks orthopoxvirus entry via heparan sulphate and regulates host antiviral pathways [4]
Abstract reading summary — source excerpts
- Opening excerpt
- Current antiviral therapies for orthopoxviruses face critical challenges, including limited efficacy and significant toxicity, which impede outbreak containment and clinical management.
- Closing excerpt
- It is particularly beneficial for immunocompromised populations in resource-limited settings during orthopoxvirus outbreaks.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (172 words)
Current antiviral therapies for orthopoxviruses face critical challenges, including limited efficacy and significant toxicity, which impede outbreak containment and clinical management. Here, we identify lactoferrin as a potent antiviral agent against multiple orthopoxvirus strains. Combination administration of lactoferrin with brincidofovir or tecovirimat demonstrated additive efficacy, suggesting a potential clinical strategy to reduce individual drug toxicity. Mechanistically, lactoferrin blocks viral entry by competitively binding to heparan sulphate proteoglycans (HSPGs). It also suppresses viral replication by regulating host antiviral pathways, including down-regulating cytokines and upregulating TGF-β-dependent antiviral signalling pathways. We identify TGFBI as a virus-responsive target regulated by lactoferrin. Lactoferrin treatment restores TGFBI expression and activates downstream MAPK/ERK and JAK2/STAT3 signalling cascades, leading to enhanced interferon production and interferon-stimulated gene (ISG) expression. In a murine vaccinia virus (VACV) infection model, lactoferrin treatment reduced lung viral loads and histological damage. These results underscore lactoferrin's distinctive dual antiviral mechanism and highlight its translational potential as a safe and cost-effective prophylactic or therapeutic agent. It is particularly beneficial for immunocompromised populations in resource-limited settings during orthopoxvirus outbreaks.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 41790953 · DOI · PMC12973843
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article C-Reactive Protein, Fecal Calprotectin, and Stool Lactoferrin for Detection of Endoscopic Activity in Symptomatic Inflammatory Bowel Disease Patients: A Systematic Review and Meta-Analysis [5]
- Research article Lactoferrin: Structure, function, denaturation and digestion [6]
- Research article Applications for α-lactalbumin in human nutrition [7]
- Research article A 100-Year Review: Advances in goat milk research [8]
- Research article Lactoferrin, a multi-functional glycoprotein: Active therapeutic, drug nanocarrier & targeting ligand [9]
- Research article Bioactive Proteins in Human Milk: Health, Nutrition, and Implications for Infant Formulas [10]
References
- Demir R, Sarıtaş S, Bechelany M, Karav S. Lactoferrin: Properties and Potential Uses in the Food Industry. . 2025. PMID 40003872 · DOI · PMC11855648
- Cao X, Cao J, Xu T, Zheng L, Dai J, Zhang X, et al.. Construction of nanodelivery system based on the interaction mechanism between ultrasound-treated soybean whey protein and quercetin: structure, physicochemical stability and bioaccessibility. . 2025. PMID 39671813 · DOI · PMC11700283
- Michielsen CMS, Lin YT, Yan J, de Jong AM, Prins MWJ. Continuous Protein Sensing Using Fast-Dissociating Antibody Fragments in Competition-Based Biosensing by Particle Motion. . 2025. PMID 40126441 · DOI · PMC12038830
- Tian L, Qin H, Li S, Zhang M, Zhuang L, Hong B, et al.. Lactoferrin blocks orthopoxvirus entry via heparan sulphate and regulates host antiviral pathways. . 2026. PMID 41790953 · DOI · PMC12973843
- Mosli MH, Zou G, Garg SK, Feagan SG, MacDonald JK, Chande N, et al.. C-Reactive Protein, Fecal Calprotectin, and Stool Lactoferrin for Detection of Endoscopic Activity in Symptomatic Inflammatory Bowel Disease Patients: A Systematic Review and Meta-Analysis. Am J Gastroenterol. 2015. PMID 25964225 · DOI
- Wang B, Timilsena YP, Blanch E, Adhikari B. Lactoferrin: Structure, function, denaturation and digestion. Crit Rev Food Sci Nutr. 2019. PMID 28933602 · DOI
- Layman DK, Lönnerdal B, Fernstrom JD. Applications for α-lactalbumin in human nutrition. Nutr Rev. 2018. PMID 29617841 · DOI · PMC5934683
- Clark S, Mora García MB. A 100-Year Review: Advances in goat milk research. J Dairy Sci. 2017. PMID 29153153 · DOI
- Elzoghby AO, Abdelmoneem MA, Hassanin IA, Abd Elwakil MM, Elnaggar MA, Mokhtar S, et al.. Lactoferrin, a multi-functional glycoprotein: Active therapeutic, drug nanocarrier & targeting ligand. Biomaterials. 2020. PMID 32932142 · DOI · PMC7480805
- Lönnerdal B. Bioactive Proteins in Human Milk: Health, Nutrition, and Implications for Infant Formulas. J Pediatr. 2016. PMID 27234410 · DOI
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-31.
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Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.