108432-90-2Relevant academic research and scientific papers
Synthesis of chimeric tetrapeptide-linked cholic acid derivatives: Impending synergistic agents
Bavikar, Sudhir N.,Salunke, Deepak B.,Hazra, Braja G.,Pore, Vandana S.,Dodd, Robert H.,Thierry, Josiane,Shirazi, Fazal,Deshpande, Mukund V.,Kadreppa, Sreenath,Chattopadhyay, Samit
, p. 5512 - 5517 (2008)
Tetrapeptides derived from glycine and β-alanine were hooked at the C-3β position of the modified cholic acid to realize novel linear tetrapeptide-linked cholic acid derivatives. All the synthesized compounds were tested against a wide variety of microorganisms (Gram-negative bacteria, Gram-positive bacteria and fungi) and their cytotoxicity was evaluated against human embryonic kidney (HEK293) and human mammary adenocarcinoma (MCF-7) cell lines. While relatively inactive by themselves, these compounds interact synergistically with antibiotics such as fluconazole and erythromycin to inhibit growth of fungi and bacteria, respectively, at 1-24 μg/mL. The synergistic effect shown by our novel compounds is due to their inherent amphiphilicity. The fractional inhibitory concentrations reported are comparable to those reported for Polymyxin B derivatives.
Cation dependence of chloride ion complexation by open-chained receptor molecules in chloroform solution
Pajewski, Robert,Ferdani, Riccardo,Pajewska, Jolanta,Li, Ruiqiong,Gokel, George W.
, p. 18281 - 18295 (2007/10/03)
Seventeen peptides, most having the sequence GGGPGGG, but differing in the C- and N-terminal ends, have been studied as anion-complexing agents. These relatively simple, open-chained peptide systems interact with both chloride and the associated cation. Changes in the N- and C-terminal side chains appear to make little difference in the efficacy of binding. NMR studies suggest that the primary interactions involve amide NH contacts with the chloride anion, and CD spectral analyses suggest a concomitant conformational change upon binding. Changes in binding constants, which are expected in different solvents, also suggest selective solvent interactions with the unbound host that helps to preorganize the open-chained peptide system. Significant differences are apparent in complexation strengths when the heptapeptide chain is shortened or lengthened or when the relative position of proline within the heptapeptide is varied.
Conformations in the Solid State and Solubility Properties of Protected Homooligopeptides of Glycine and β-Alanine
Narita, Mitsuaki,Doi, Masamitsu,Kudo, Koji,Terauchi, Yusuke
, p. 3553 - 3558 (2007/10/02)
IR spectroscopic conformational analyses of Boc-Glyn-OBzl (n=3-7) and Boc-(β-Ala)n-OBzl (n=3-8) were performed in the solid state, suggesting the occurrence of the β-sheet structure in the higher oligomers (n=5-8).Solubility data ind
