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  • Beilstein-Institut  (1)
  • International Union of Crystallography (IUCr)  (1)
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    Electronic Resource
    Electronic Resource
    An oxazol-5(4H)-one from benzyloxycarbonyl-(Aib)4-OH (2000)
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 695-696 
    Details
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Benzyl N-[8-(4,4-dimethyl-5-oxo-4,5-dihydrooxazol-2-yl)-2,5,5,8-tetramethyl-3,6-dioxo-4,7-diazanon-2-yl]carbamate, C24H34N4O6, an oxazol-5(4H)-one from N-α-benzyloxycarbonyl-(Aib)4-OH (Aib = α-aminoisobutyryl) represents the longest peptide oxazolone so far characterized by X-ray diffraction. The overall geometry of the oxazolone ring compares well with literature data. The Aib(1) and Aib(2) residues are folded into a type III β-bend, while the conformation adopted by Aib(3), preceding the oxazolone moiety, is semi-extended. The disposition of the oxazolone ring relative to the preceding residue is stabilized by C—H...N and C—H...O intramolecular interactions.Alternative name: 4,4-dimethyl-2-[1-(phenylmethoxycarbonyl-2-methylalanyl-2-methylalanylamino)-1-methylethyl]oxazol-5(4H)-one.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0108270100003413
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    Paper (German National Licenses)
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    Partial thioamide scan on the lipopeptaibiotic trichogin GA IV. Effects on folding and bioactivity (2012)
    Beilstein-Institut
    Details
    Publication Date: 2012-07-24
    Description: Backbone modification is a common chemical tool to control the conformation of linear peptides and to explore potentially useful effects on their biochemical and biophysical properties. The thioamide, ψ[CS-NH], group is a nearly isosteric structural mimic of the amide (peptide) functionality. In this paper, we describe the solution synthesis, chemical characterization, preferred conformation, and membrane and biological activities of three, carefully selected, peptide analogues of the lipopeptaibiotic [Leu11-OMe] trichogin GA IV. In each analogue, a single thioamide replacement was incorporated. Sequence positions near the N-terminus, at the center, and near the C-terminus were investigated. Our results indicate that (i) a thioamide linkage is well tolerated in the overall helical conformation of the [Leu11-OMe] lipopeptide analogue and (ii) this backbone modification is compatible with the preservation of its typical membrane leakage and antibiotic properties, although somewhat attenuated.
    Print ISSN: 2195-951X
    Electronic ISSN: 1860-5397
    Topics: Chemistry and Pharmacology
    Published by Beilstein-Institut
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