4.7 Article

Cytotoxicity of apo bovine α-lactalbumin complexed with La3+ on cancer cells supported by its high resolution crystal structure

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SCIENTIFIC REPORTS
卷 9, 期 -, 页码 -

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NATURE PUBLISHING GROUP
DOI: 10.1038/s41598-018-38024-1

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资金

  1. DST/SERB [EMR/2014/000985, SB/S2/JCB-066/2015]
  2. IIT Bombay for Institute Chair Professorship
  3. Ramalingaswami Re-entry Fellowship, DBT
  4. UGC
  5. DBT [BT/PR3871/MED/30/830/2012]

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Cancer remains one of the biggest threats to human society. There are massive demands for compounds to selectively kill cancerous cells. Earlier studies have shown that bovine alpha-lactalbumin made lethal to tumor cells (BAMLET) becomes cytotoxic against cancer cells in complex with oleic acid {Hoque, M. et. al., PLoSOne 8, e68390 (2013)}. In our study, we obtained bovine alpha-lactalbumin complexed with lanthanum ion (La3+-B-alpha-LA) and determined its high resolution crystal structure. The natural calcium binding site of bovine a-lactalbumin is replaced by lanthanum. The La3+ complex formation by B-alpha-apo- LA was also supported by various biophysical methods. Interestingly, our complex, La3+-B-alpha-LA exhibits much greater anticancer activity against breast cancer cells as compared to the reported BAMLET-oleic acid complex. This study shows that La3+-B-alpha-LA complex is preferentially more toxic to MCF-7 cells as compared to KB (oral cancer) and HeLa (cervical) cells, while almost non-toxic to the healthy cells that we studied. Our data indicates that the cytotoxicity of La3+-B-alpha-LA against cancer cells is through apoptotic path way. The higher anticancer activity of La3+-B-alpha-LA is attributable to the requisite structural changes induced in the protein by La3+ binding as supported by the crystal structure of the complex.

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