- Selective removal of fluorenylmethoxycarbonyl (FMOC) groups under mild conditions
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N-Fluorenylmethoxycarbonyl groups may be removed by potassium fluoride/18- crown-6 in the presence of methyl, ethyl, tert-butyl, benzyl, and p- methoxybenzyl esters.
- Jiang,Li,Joullie
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Read Online
- Development of supramolecular organo-gel based on tripeptide skeletons
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Boc-Ser-Val-Gly-OCH2Ph (31) showed high gelation abilities in the aromatic solvents, particularly in toluene. The minimum gelation concentration of 31 in toluene was 10 mg/ml, suggesting that 2500 molecules of toluene were immobilized by each m
- Azuma, Eriko,Kuramochi, Kouji,Tsubaki, Kazunori
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p. 680 - 684
(2010/07/15)
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- A templating approach for monodisperse self-assembled organic nanostructures
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The precise structural control is known for self-assembly into closed spherical structures (e.g., micelles), but similar control of open structures is much more challenging. Inspired by natural tobacco mosaic virus, we present the use of a rigid-rod template to control the size of a one-dimensional self-assembly. We believe that this strategy is novel for organic self-assembly and should provide a general approach to controlling size and dimension. Copyright
- Bull, Steve R.,Palmer, Liam C.,Fry, Nathaniel J.,Greenfield, Megan A.,Messmore, Benjamin W.,Meade, Thomas J.,Stupp, Samuel I.
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p. 2742 - 2743
(2008/09/20)
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- Thioamides: Synthesis, stability, and immunological activities of thioanalogues of imreg. Preparation of new thioacylating agents using fluorobenzimidazolone derivatives
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Imreg (Tyr1-Gly2-Gly3) is a well-known immunostimulant. However, it possesses a short half-life. Stabilized analogues of Imreg were prepared by a regioselective insertion in which peptide bonds at position 1,2 or 2,3 were
- Zacharie, Boulos,Lagraoui, Mouna,Dimarco, Marika,Penney, Christopher L.,Gagnon, Lyne
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p. 2046 - 2052
(2007/10/03)
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- The L-Proline Residue as a 'Break-point' in Metal - Peptide Systems
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Results are reported of a potentiometric and spectrophotometric study of the H+ and Cu2+ complexes of the tetrapeptides X-Gly-Gly-Gly, Gly-X-Gly-Gly, Gly-Gly-X-Gly, and Gly-Gly-Gly-X where X is the proline (Pro) and sarcosine (Sar) residue (Gly=glycine).All the tetrapeptides (HL) form the series of complexes , -1L>, -2L>, and -3L> (charges omitted).The ligands Gly-X-Gly-Gly also form the bis-complex, .When inserted in a peptide chain the Pro and Sar residues cannot co-ordinate to Cu2+ through their peptide nitrogens since they do not possess ionizable protons.In addition the Pro residue tends to force the peptide chain to form a 'β-turn' and so adopt a 'bent' conformation.These studies demonstrate the formation of a large chelate ring when tetrapeptides containing Pro (and , to a smaller extent, Sar) in the second or third positions co-ordinate to Cu2+.This ring spans the terminal residues of the peptide chain and locks the peptide into a 'bent' or 'horse-shoe' shaped conformation.Cu2+ could therefore play an important role in activating oligopeptides (e.g. neuropeptides) containing proline.
- Pettit, Leslie D.,Steel, Ian,Formicka-Kozlowska, Grazyna,Tatarowski, Tomasz,Bataille, Michael
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p. 535 - 540
(2007/10/02)
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