vinorelbine and phomopsin

vinorelbine has been researched along with phomopsin* in 2 studies

Other Studies

2 other study(ies) available for vinorelbine and phomopsin

ArticleYear
One-pot synthesis of vinca alkaloids-phomopsin hybrids.
    Journal of medicinal chemistry, 2014, Jun-26, Volume: 57, Issue:12

    Hybrids of vinca alkaloids and phomopsin A have been elaborated with the aim of interfering with the "vinca site" and the "peptide site" of the vinca domain in tubulin. They were synthesized by an efficient one-pot procedure that directly links the octahydrophomopsin lateral chain to the velbenamine moiety of 7'-homo-anhydrovinblastine. In their modeled complexes with tubulin, these hybrids were found to superimpose nicely on the tubulin-bound structures of vinblastine and phomopsin A. This good matching can account for the fact that two of them are very potent inhibitors of microtubules assembly and are cytotoxic against four cancer cell lines.

    Topics: Antineoplastic Agents; Cell Line, Tumor; Drug Screening Assays, Antitumor; Humans; Models, Molecular; Mycotoxins; Tubulin; Tubulin Modulators; Vinblastine

2014
Synthesis and biological evaluation of vinca alkaloids and phomopsin hybrids.
    Journal of medicinal chemistry, 2009, Jan-08, Volume: 52, Issue:1

    Ten hybrids of vinca alkaloids and phomopsin A have been synthesized by linking the octahydrophomopsin lateral chain to the tertiary amine of the cleavamine moiety of anhydrovinblastine (AVLB) and vinorelbine. These compounds have been elaborated in order to obtain original products that may interfere with both binding sites of vinblastine (VLB) and phomopsin in tubulin. Although NMR and molecular modeling studies have shown that the orientation of the added peptide chains of these hybrids is not the same as those of phomopsin A, most of them are very potent inhibitors of microtubules assembly and they present good cytotoxicity against KB cell line. These interesting biological activities may eventually be explained by the fact that their lateral chain resides in a pocket distinct from that of the phomopsin A peptide, at the interface of tubulins beta and alpha.

    Topics: Antimitotic Agents; Cell Death; Cell Line; Inhibitory Concentration 50; Magnetic Resonance Spectroscopy; Microtubules; Molecular Structure; Mycotoxins; Tubulin; Tubulin Modulators; Vinblastine; Vinca Alkaloids; Vinorelbine

2009