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- W2531596682 abstract "Bovine α-lactalbumin (BLA) forms cytotoxic complexes with oleic acid (OA) that perturbs tumor cell membranes, but molecular determinants of these membrane-interactions remain poorly understood. Here, we aim to obtain molecular insights into the interaction of BLA/BLA-OA complex with model membranes. We characterized the folding state of BLA-OA complex using tryptophan fluorescence and resolved residue-specific interactions of BLA with OA using molecular dynamics simulation. We integrated membrane-binding data using a voltage-sensitive probe and molecular dynamics (MD) to demonstrate the preferential interaction of the BLA-OA complex with negatively charged membranes. We identified amino acid residues of BLA and BLA-OA complex as determinants of these membrane interactions using MD, functionally corroborated by uptake of the corresponding α-LA peptides across tumor cell membranes. The results suggest that the α-LA component of these cytotoxic complexes confers specificity for tumor cell membranes through protein interactions that are maintained even in the lipid complex, in the presence of OA." @default.
- W2531596682 created "2016-10-21" @default.
- W2531596682 creator A5021651777 @default.
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- W2531596682 date "2016-10-12" @default.
- W2531596682 modified "2023-10-16" @default.
- W2531596682 title "Protein-dependent Membrane Interaction of A Partially Disordered Protein Complex with Oleic Acid: Implications for Cancer Lipidomics" @default.
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- W2531596682 doi "https://doi.org/10.1038/srep35015" @default.
- W2531596682 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5059734" @default.
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- W2531596682 hasPublicationYear "2016" @default.
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