Abstract
Four previously undescribed cyclic peptides, reniochpeptins A-D (1-4), were isolated from the marine sponge Reniochalina sp. Their structures were elucidated through comprehensive spectroscopic analyses and a modified advanced Marfey's method. This method utilized ultra-high-performance liquid chromatography coupled with tandem multiple reaction monitoring mass spectrometry, employing a CORTECS T3 column to achieve simultaneous separation of derivatized L-Leu, L-Ile, L-allo-Ile, D-Leu, D-Ile, and D-allo-Ile within 25min in a single analytical run. Reniochpeptin A displayed moderate inhibitory activity against NCI-H460cells, with an IC50 value of 4.7μM, by inducing cell cycle arrest at the G2/M phase and promoting apoptosis.
Published Version
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