ArticleFEBS open bio2015
The cytotoxicity of BAMLET complexes is due to oleic acid and independent of the α-lactalbumin component.
Article in FEBS open bio, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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
10 citing papers in PubMed, 39 citations in OpenAlex.
- Anticancer Nanoparticle Carriers of the Proapoptotic Protein CytochromePharmaceutics · 2025Review
- Nutrition, production, and processing of virgin omega-3 polyunsaturated fatty acids in dairy: An integrative review.Heliyon · 2024Review
- Chicken embryo model forInternational journal of pharmaceutics: X · 2023Article
- Diagnosis and Rationale for Action against Cow's Milk Allergy (DRACMA) Guidelines update - III - Cow's milk allergens and mechanisms triggering immune activation.The World Allergy Organization journal · 2022Article
- Using BAMLET complex in a functional spreadable cheese elaborated with bovine colostrum.Journal of food science and technology · 2021Article
- α-Lactalbumin, Amazing Calcium-Binding Protein.Biomolecules · 2020Review
- The Use of Human, Bovine, and Camel Milk Albumins in Anticancer Complexes with Oleic Acid.The protein journal · 2018Article
- Applications for α-lactalbumin in human nutrition.Nutrition reviews · 2018Review
- BAMLET kills chemotherapy-resistant mesothelioma cells, holding oleic acid in an activated cytotoxic state.PloS one · 2018Article
- Liprotides kill cancer cells by disrupting the plasma membrane.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Lipid-protein complexes comprised of oleic acid (OA) non-covalently coupled to human/bovine α-lactalbumin, named HAMLET/BAMLET, display cytotoxic properties against cancer cells. However, there is still a substantial debate about the role of the protein in these complexes. To shed light into this, we obtained three different BAMLET complexes using varying synthesis conditions. Our data suggest that to form active BAMLET particles, OA has to reach critical micelle concentration with an approximate diameter of 250 nm. Proteolysis experiments on BAMLET show that OA protects the protein and is probably located on the surface, consistent with a micelle-like structure. Native or unfolded α-lactalbumin without OA lacked any tumoricidal activity. In contrast, OA alone killed cancer cells with the same efficiency at equimolar concentrations as its formulation as BAMLET. Our data show unequivocally that the cytotoxicity of the BAMLET complex is exclusively due to OA and that OA alone, when formulated as a micelle, is as toxic as the BAMLET complex. The contradictory literature results on the cytotoxicity of BAMLET might be explained by our finding that it was imperative to sonicate the samples to obtain toxic OA.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.