ArticleProtein science : a publication of the Protein Society2004
Conformational analysis of HAMLET, the folding variant of human alpha-lactalbumin associated with apoptosis.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- HAMLET in human milk is resistant to digestion and carries essential free long chain polyunsaturated fatty acids and oleic acid.Food chemistry · 2023Article
- Cytotoxic Lactalbumin-Oleic Acid Complexes in the Human Milk Diet of Preterm Infants.Nutrients · 2021Review
- Protein-lipid complexes: molecular structure, current scenarios and mechanisms of cytotoxicity.RSC advances · 2019Review
- Cytotoxicity of apo bovine α-lactalbumin complexed with LaScientific reports · 2019Article
- Protein-dependent Membrane Interaction of A Partially Disordered Protein Complex with Oleic Acid: Implications for Cancer Lipidomics.Scientific reports · 2016Article
- Using THz Spectroscopy, Evolutionary Network Analysis Methods, and MD Simulation to Map the Evolution of Allosteric Communication Pathways in c-Type Lysozymes.Molecular biology and evolution · 2016Article
- Molecular mechanisms of the cytotoxicity of human α-lactalbumin made lethal to tumor cells (HAMLET) and other protein-oleic acid complexes.The Journal of biological chemistry · 2013Article
- Autophagy protein p62/SQSTM1 is involved in HAMLET-induced cell death by modulating apotosis in U87MG cells.Cell death & disease · 2013Article
- Oleic acid may be the key contributor in the BAMLET-induced erythrocyte hemolysis and tumoricidal action.PloS one · 2013Article
- Influence of pH on the structure and oleic acid binding ability of bovine α-lactalbumin.The protein journal · 2012Article
- Interaction of antitumor alpha-lactalbumin-oleic acid complexes with artificial and natural membranes.Journal of bioenergetics and biomembranes · 2009Article
- Protection Against Dimethylbenz[a] Anthracene-Induced Breast Cancer in Female Rats by α-Lactalbumin.International journal of cancer and oncologyArticle
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Authors and funding
8 authors.
Funding
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Abstract
A combination of hydrogen/deuterium (H/D) exchange and limited proteolysis experiments coupled to mass spectrometry analysis was used to depict the conformation in solution of HAMLET, the folding variant of human alpha-lactalbumin, complexed to oleic acid, that induces apoptosis in tumor and immature cells. Although near- and far-UV CD and fluorescence spectroscopy were not able to discriminate between HAMLET and apo-alpha-lactalbumin, H/D exchange experiments clearly showed that they correspond to two distinct conformational states, with HAMLET incorporating a greater number of deuterium atoms than the apo and holo forms. Complementary proteolysis experiments revealed that HAMLET and apo are both accessible to proteases in the beta-domain but showed substantial differences in accessibility to proteases at specific sites. The overall results indicated that the conformational changes associated with the release of Ca2+ are not sufficient to induce the HAMLET conformation. Metal depletion might represent the first event to produce a partial unfolding in the beta-domain of alpha-lactalbumin, but some more unfolding is needed to generate the active conformation HAMLET, very likely allowing the protein to bind the C18:1 fatty acid moiety. On the basis of these data, a putative binding site of the oleic acid, which stabilizes the HAMLET conformation, is proposed.
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