The zeolites are porous solid structures characterized by a particular framework of aluminosilicates, in which the incorporation of the Al⁺³ ions generates an excess of negative charge compensated by cations (usually alkali or alkali earth) or protons. In the latter case, they are employed as catalysts for a wide variety of reactions, such as dehydration, skeletal isomerization and cracking, while the catalytic activity of basic zeolites has not found, up to now, any industrial or whatever relevant application in chemical processes. In the present review, we firstly intend to give an overview of the fundamental chemical composition, as well as the structural features of the zeolite framework. The purpose of this paper is to analyze their key properties as acid, both Lewis and Brønsted, and basic solid support. Their application as catalysts is discussed by reviewing the already published works in that field, and a final remark of their still unexplored potential as green, mild, and selective catalyst is also reported.

The CXCR4/CXCL12 axis plays a role in cancer metastases, stem cell mobilization and chemosensitization. Proof of concept for efficient CXCR4 inhibition has been demonstrated in stem cell mobilization prior to autologous transplantation in hematological malignancies. Nevertheless CXCR4 inhibitors suitable for prolonged use as required for anticancer therapy are not available. To develop new CXCR4 antagonists a rational, ligand-based approach was taken, distinct from the more commonly used development strategy. A three amino acid motif (Ar-Ar-X) in CXCL12, also found in the reverse orientation (X-Ar-Ar) in the vMIP-II inhibitory chemokine formed the core of nineteen cyclic peptides evaluated for inhibition of CXCR4-dependent migration, binding, P-ERK1/2-induction and calcium efflux. Peptides R, S and I were chosen for evaluation in in vivo models of lung metastases (B16-CXCR4 and KTM2 murine osteosarcoma cells) and growth of a renal cells xenograft. Peptides R, S, and T significantly reduced the association of the 12G5-CXCR4 antibody to the receptor and inhibited CXCL12-induced calcium efflux. The four peptides efficiently inhibited CXCL12-dependent migration at concentrations as low as 10 nM and delayed CXCL12-mediated wound healing in PES43 human melanoma cells. Intraperitoneal treatment with peptides R, I or S drastically reduced the number of B16-CXCR4-derived lung metastases in C57/BL mice. KTM2 osteosarcoma lung metastases were also reduced in Balb/C mice following CXCR4 inhibition. All three peptides significantly inhibited subcutaneous growth of SN12C-EGFP renal cancer cells. A novel class of CXCR4 inhibitory peptides was discovered. Three peptides, R, I and S inhibited lung metastases and primary tumor growth and will be evaluated as anticancer agents.

Chemical modification of pectin was successfully accomplished as a solvent free process. It involved acylation of alcoholic functions of the polysaccharide by using several fatty acid anhydrides. The reaction was performed by simply mixing the reagents with a catalytic amount of the inorganic base potassium carbonate and heating the obtained mixture at a temperature of 160 °C. The desired esters were fully characterized by NMR and FT-IR spectroscopy.

Microwave-assisted solvent-free modification of pectin was successfully accomplished, consisting in the esterification of several fatty acids by pectin alcoholic functions. The reaction was performed by simply mixing the reagents with a catalytic amount of the inorganic base (potassium carbonate) and irradiating the obtained mixture with microwaves for a short time (3–6 min). The replacement of the traditional heating with a microwave source allowed the development of a new synthetic protocol which provided increased yield of the final products, since it eliminates the small amount of degraded polysaccharide produced during traditional oil bath heating. The desired esters were fully characterized by FT-IR spectroscopy and thermogravimetric analysis.

Purpose: To test whether a novel bifunctional chimeric peptide comprising a cyclic Arg-Gly-Asp pentapeptide covalently bound to an echistatin domain can discriminate α_vβ₃ from α_vβ₅ integrin, thus allowing the in vivo selective visualization of α_vβ₃ expression by single-photon and positron emission tomography (PET) imaging.