108432-95-7Relevant 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
supporting information; experimental part, p. 5512 - 5517 (2009/06/18)
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.
Cyclic β-tetra- and pentapeptides: Synthesis through on-resin cyclization and conformational studies by X-ray, NMR and CD spectroscopy and theoretical calculations
Buettner, Frank,Norgren, Anna S.,Zhang, Suode,Prabpai, Samran,Kongsaeree, Palangpon,Arvidsson, Per I.
, p. 6145 - 6158 (2007/10/03)
The solution-phase synthesis of the simplest cyclic β-tetrapeptide, cyclo(β-Ala)4 (4), as well as the solid-phase syntheses through side chain anchoring and on-resin cyclization of the cyclic β3- tetrapeptide cyclo(-β3hPheβ33hLeu- β3hLys-β3hGln-) (14) and the first cyclic β3-pentapeptide cyclo(-β3hVal- β3hPhe-β3hLeu-β3hLys- β3hLys-) (19) are reported. Extensive computational as well as spectroscopic studies, including X-ray and NMR spectroscopy, were undertaken to determine the preferred conformations of these unnatural oligomers in solution and in the solid state. cyclo(β-Ala)4 (4) with no chiral side chains is shown to exist as a mixture of rapidly interchanging conformers in solution, whereas inclusion of chiral side chains in the cyclo- β3-tetrapeptide causes stabilization of one dominating conformer. The cyclic β3-pentapeptide on the other hand shows larger conformational freedom. The X-ray structure of achiral cyclo(β-Ala)4 (4) displays a Ci-symmetrical 16-membered ring with adjacent C=O and N-H atoms pointing pair wise up and down with respect to the ring plane. CD spectroscopic examinations of all cyclic β-peptides were undertaken and revealed results valuable as starting point for further structural investigations of these entities.
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
