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A new compound, Na(HINA)2(NH4)2[PMo10V2O40]·14H2O (1) (INA = isonicotinic acid) was synthesized and characterized structurally by elemental analysis, IR spectroscopy, and TG. Bisubstituted molybdovanadophosphate anions have typical Keggin anion structure and are linked weakly by Na+ ions into an anionic chain along crystallographic b axis. Protonated INA cations form another supramolecular cationic chain also along crystallographic b axis. Two chains, water molecules, and ammonium ions form the 3D supramolecular architecture through hydrogen bonds. The compound has an excellent catalytic activity to starch oxidation. The detailed study gives optimum reaction condition. [ABSTRACT FROM AUTHOR]

In the present study, the hydrophobicity of a 26-residue α-helical peptide (peptide P) was altered to study the effects of peptide hydrophobicity on the mechanism of action of cationic anticancer peptides. Hydrophobicity of the nonpolar face of the peptides was shown to correlate with peptide helicity. The self-association ability of peptides in aqueous environment, determined by the reversed-phase high performance liquid chromatography temperature profiling, showed strong influence on anticancer activity. The peptide analogues with greater hydrophobicity showed stronger anticancer activity determined by IC(50) values with a necrotic-like membrane disruption mechanism. Peptide analogues exhibited high specificity against cancer cells and much higher anticancer activity than widely-used anticancer chemical drugs. The mechanism of action of anticancer peptides was also investigated. The hydrophobicity of peptides plays a crucial role in the mechanism of action against cancer cells, which could present a way, using a de novo design approach, to create anticancer peptides as potential therapeutics in clinical practices., (©2011 AACR.)