N-Benzyloxyethyl cyclic alpha-peptoids of various size were prepared and their conformational features were investigated by means of computational, spectroscopic, and X-ray crystallographic studies.

Azumamide E, a cyclotetrapeptide isolated from the sponge Mycale izuensis, is the most powerful carboxylic acid containing natural histone deacetylase (HDAC) inhibitor known to date. In this paper, we describe design and synthesis of two stereochemical variants of the natural product. These compounds have allowed us to clarify the influence of side chain topology on the HDAC-inhibitory activity. The present contribution also reveals the identity of the recognition pattern between azumamides and the histone deacetylase-like protein (HDLP) model receptor and reports the azumamide E unprecedented isoform selectivity on histone deacetylases class subtypes. From the present studies, a plausible model for the interaction of azumamides with the receptor binding pocket is derived, providing a framework for the rational design of new cyclotetrapeptide-based HDAC inhibitors as antitumor agents.

1,3-Alternate cationic calix[4]arene proved highly selective for proton/halogens symport transport and showed antiproliferative activity against murine monocyte/macrophage J774.A1 cancer cells.

The synthesis of a new class of amphiphilic calix[4]arene-based ionophores, relying on direct reductive amination as a key step, and the evaluation of their H+ and Na+ transporting properties is described.

Azumamides A (1) and E (5) belong to the rare class of histone deacetylase (HDAC) inhibitors, typified by a cyclic tetrapeptide core. HDAC inhibitors are unique lead compounds for the development of specific, noncytotoxic antitumor antibiotics. We have developed a successful protocol for the solution-phase synthesis of azumamides A (1) and E (5),\ud establishing unequivocally the configurations of the azumamides, and presented a three-dimensional NMR solution state\ud structure of azumamide E (5)