Dataset for: Peptide fragments of Hsp70 modulate its chaperone activity and sensitize tumor cells to anti-cancer drug

Most of Hsp70 chaperone inhibitors exert anti-cancer effects and though their toxicity prompted us to employ peptide fragments of the chaperone as its safer modulators and as complements to customary drugs. One of such peptides, ICit-2 was found to inhibit substrate-binding and refolding activities of the chaperone. Using various approaches, we established that ICit-2 binds Hsp70 that may explain the compound inhibitory action. ICit-2 penetrates living A-431 cancer cells and in combination with doxorubicin enhances the drug cytotoxicity and growth inhibitory effect. Similarly, using B16 mouse melanoma model we found that ICit-2 inhibited the rate of tumor growth by 48% compared with the doxorubicin alone proving that the peptide can be employed to sensitize resistant tumors to cytostatic medicines.