Transition from vesicles to nanofibres in the enzymatic self-assemblies of an amphiphilic peptide as an antitumour drug carrier

The enzyme-responsive self-assembly of the amphiphilic peptide A6K2 and the release of an antitumour drug (DOX) from the self-assembled nanovesicles of the amphiphilic peptide.

The antitumour drug 7-ethyl-10-hydroxycamptothecin monohydrate and its solid-state hydrolysis mechanism on heating

7-Ethyl-10-hydroxycamptothecin [systematic name: (4S)-4,11-diethyl-4,9-dihydroxy-1H-pyrano[3′,4′:6,7]indolizino[1,2-b]quinoline-3,14(4H,12H)-dione, SN-38] is an antitumour drug which exerts activity through the inhibition of topoisomerase I. The crystal structure of SN-38 as the monohydrate, C22H20N2O5·H2O, reveals that it is a monoclinic crystal, with one SN-38 molecule and one water molecule in the asymmetric unit. When the crystal is heated to 473 K, approximately 30% of SN-38 is hydrolyzed at its lactone ring, resulting in the formation of the inactive carboxylate form. The molecular arrangement around the water molecule and the lactone ring of SN-38 in the crystal structure suggests that SN-38 is hydrolyzed by the water molecule at (x,y,z) nucleophilically attacking the carbonyl C atom of the lactone ring at (x − 1,y,z − 1). Hydrogen bonding around the water molecules and the lactone ring appears to promote this hydrolysis reaction: two carbonyl O atoms, which are hydrogen bonded as hydrogen-bond acceptors to the water molecule at (x,y,z), might enhance the nucleophilicity of this water molecule, while the water molecule at (−x,y + {1\over 2}, −z), which is hydrogen bonded as a hydrogen-bond donor to the carbonyl O atom at (x − 1,y,z − 1), might enhance the electrophilicity of the carbonyl C atom.

Towards understanding P-gp resistance: a case study of the antitumour drug cabazitaxel

A structural and Hirshfeld surface study of five forms of the antitumour drug cabazitaxel suggests key factors contributing to its poor affinity to P-gp.