@article {42993,
	title = {Protein-dependent membrane interaction of a partially disordered protein complex with oleic acid : Implications for cancer lipidomics},
	journal = {Scientific Reports},
	volume = {6},
	year = {2016},
	month = {OCT},
	abstract = {<p>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.</p>},
	doi = {10.1038/srep35015},
	author = {Chaudhuri, Arunima and Prasanna, Xavier and Agiru, Priyanka and Chakraborty, Hirak and Rydstrom, Anna and Ho, James C. S. and Svanborg, Catharina and Sengupta, Durba and Chattopadhyay, Amitabha}
}
@article {48360,
	title = {Preface to special issue on protein-mediated membrane remodeling},
	journal = {Journal of Membrane Biology},
	volume = {255},
	year = {2022},
	month = {DEC},
	pages = {633-635},
	type = {Editorial Material},
	issn = {0022-2631},
	doi = {10.1007/s00232-022-00273-7},
	author = {Chakraborty, Hirak and Sengupta, Durba}
}
