- Dynamic interface imprinting: High-affinity peptide binding sites assembled by analyte-induced recruiting of membrane receptors
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Come together: Dynamic molecular recognition events at biological membrane receptors play a key role in cell signaling. Artificial membranes have been prepared with embedded synthetic receptors which dynamically arrange and selectively respond to external stimuli, such as, small peptide ligands. Copyright
- Gruber, Benjamin,Balk, Stefan,Stadlbauer, Stefan,Koenig, Burkhard
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supporting information
p. 10060 - 10063,4
(2012/12/12)
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- Dynamic interface imprinting: High-affinity peptide binding sites assembled by analyte-induced recruiting of membrane receptors
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Come together: Dynamic molecular recognition events at biological membrane receptors play a key role in cell signaling. Artificial membranes have been prepared with embedded synthetic receptors which dynamically arrange and selectively respond to external stimuli, such as, small peptide ligands. Copyright
- Gruber, Benjamin,Balk, Stefan,Stadlbauer, Stefan,K?nig, Burkhard
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supporting information
p. 10060 - 10063
(2013/01/15)
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- Deprotection of N-tert-butoxycarbonyl (Boc) groups in the presence of tert-butyl esters
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Deprotection of Boc groups in the presence of tert-butyl esters was achieved by using concentrated H2SO4 (1.5-3.0 equiv.) in tBuOAc or MeSO3H (1.5-3.0 equiv.) in tBuOAc:CH2Cl2 (4:1 v/v). The yields ranged from 70 to 100% for a variety of amino acid and dipeptide substrates. (C) 2000 Elsevier Science Ltd.
- Lin,Lanza T.,De Laszlo,Truong,Kamenecka,Hagmann
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p. 7013 - 7016
(2007/10/03)
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- Heterocyclic analogues of L-citrulline as inhibitors of the isoforms of nitric oxide synthase (NOS) and identification of N(δ)-(4,5-dihydrothiazol-2-yl)ornithine as a potent inhibitor
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L-Thiocitrulline is a known potent inhibitor of several isoforms of nitric oxide synthase (NOS). To explore the structure-activity relationships (SARs) for this molecule in more depth than has previously been reported, three analogues substituted at the sulphur of the isothioureas have been synthesised. In two of these, the S-substituent was 'tied back' sterically by cyclisation to the nitrogen remote from the amino-acid unit. N(δ)-(4,5-Dihydrothiazol-2-yl)ornithine was identified as an inhibitor of rat inducible and constitutive isoforms of NOS and of a constitutive NOS derived from a human tumour xenograft. Analogous N(δ)-(thiazol-2-yl)ornithines were less active, whereas the corresponding N(δ)-(oxazol-2-yl)ornithine and N(δ)-(pyrimidin-2-yl)ornithine failed completely to inhibit NOS. A new efficient preparation of the critical synthetic intermediate, N(α)-Boc-thiocitrulline t-butyl ester, has been developed. Further exploration of the SAR with 2-amino-5-(heterocyclylthio)pentanoic acids (synthesised from 2-(Boc-amino)-5-bromopentanoic acid t-butyl ester), with N-(4-aminobutyl)thiourea and with 2-(4-aminobutylamino)-4,5-dihydrothiazole enabled refinement of our previous model for binding of the substrate, L-arginine, and the inhibitors to NOS.
- Ulhaq, Saraj,Chinje, Edwin C.,Naylor, Matthew A.,Jaffar, Mohammed,Stratford, Ian J.,Threadgill, Michael D.
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p. 1787 - 1796
(2007/10/03)
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- Lysine and Ornithine Analogues of Methotrexate as Inhibitors of Dihydrofolate Reductase
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The ornithine (6a) and lysine (6b) analogues of methotrexate (1) have been synthesized via condensation of 4-amino-4-deoxy-N10-methylpteroic acid (2) with Nδ-carbobenzoxy-L-ornithine tert-butyl ester (3a) and Nε-carbobenzo
- Kempton, Robert J.,Black, Angelique M.,Anstead, Gregory M.,Kumar, A. Ashok,Blankenship, Dale T.,Freisheim, James H.
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p. 475 - 477
(2007/10/02)
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