ArticleThe protein journal2012
Influence of pH on the structure and oleic acid binding ability of bovine α-lactalbumin.
Article in The protein journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed.
- Resveratrol Effect on α-Lactalbumin Thermal Stability.Biomedicines · 2024Article
- Preparation of Gum Arabic-Maltose-Pea Protein Isolate Complexes for 1-Octacosanol Microcapsule: Improved Storage Stability, Sustained Release in the Gastrointestinal Tract, and Its Effect on the Lipid Metabolism of High-Fat-Diet-Induced Obesity Mice.Foods (Basel, Switzerland) · 2022Article
- Protein-lipid complexes: molecular structure, current scenarios and mechanisms of cytotoxicity.RSC advances · 2019Review
- Using Liprotides to Deliver Cholesterol to the Plasma Membrane.The Journal of membrane biology · 2018Article
- 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
- Common solvents for making extraction of allergenic proteins from plants' pollens for prick tests and related factors: a technical review.Electronic physician · 2017Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The biological function of α-lactalbumin (α-LA) depends on its conformation. α-LA can adopt a stable intermediate state induced by heating or pH change. This intermediate state associates with oleic acid (OA) to form an anti-tumor complex. The effect of temperature on the formation the complex has been studied, whereas the effect of pH on complex formation remains unresolved. The effect of pH on tryptophan residues, hydrophobic clusters and secondary structure of Ca(2+)-depleted bovine α-LA (BLA) was studied by fluorescence spectroscopy and circular dichroism. BLA was found to adopt a more flexible conformation between pH 7.0 and 9.0 with buried hydrophobic clusters. The binding ability of α-LA towards OA and the anti-tumor activity of the corresponding complex were also studied. BLA was found to bind more OA over the pH range of 7.0-9.0 and the corresponding complexes showed a higher anti-tumor activity than those complexes formed under acidic conditions. Our study indicates that alkaline pH aided the formation of the complex as well as its anti-tumor activity. We also propose a possible characteristic structure that facilitates binding of OA.
Indexed as
Identifiers
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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.