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  • 1
    ISSN: 1600-5368
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The structure of the synthetic protected tripeptide methyl 1-{N-[N-(benzyloxycarbonyl)-α-aminoisobutyryl]-α-aminoisobutyryl}-4-hydroxypyrrolidine-2-carboxylate (Z–Aib–Aib–Hyp–OMe) ethanol solvate, C22H31N3O7.C2H6O, was determined by X-ray crystallography. The peptide backbone adopts a conformation, which lies in the right-handed helical region for Aib1, in the left-handed helical region for Aib2 and in the semi-extended region for Hyp3.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. e578-e579 
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The structure of the synthetic protected dipeptide (Z)-Pro–Leuol [systematic name: benzyl 2-(1-hydroxymethyl-3-methylbutylaminocarbonyl)pyrrolidine-1-carboxylate], C19H28N2O4, was determined by X-ray crystallography. The peptide adopts a novel backbone conformation compared with other longer oligopeptides containing Pro–Leuol.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Chirality 5 (1993), S. 385-392 
    ISSN: 0899-0042
    Keywords: D-amino acids ; bacterial starter cultures ; amino acid racemases ; nutrition ; gas chromatography ; chiral stationary phases ; Chirasil-Val ; Lipodex ; cyclodextrins ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Bacteria of the genera Acetobacter, Bifidobacterium, Brevibacterium, Lactobacillus, Micrococcus, Propionibacterium, and Streptococcus, which are used as so-called starter cultures for the large-scale production of fermented foods and beverages in food biotechnology, have been investigated for the chirality of their amino acids (AA) by gas chromatography (GC). Bacteria were grown in complex media, centrifuged, and washed with 0.85% aqueous NaCl. Aliquots were totally hydrolyzed (6 M HCl, 110°C, 18 h), or extracted with 70% aqueous ethanol in order to isolated free AA. The AA were adsorbed on Dowex WX 8 cation-exchanger, eluted with 4 M ammonia and converted into their N(O)-trifluoroacetyl(TFA) 2-propyl esters or TFA methyl esters. The AA derivatives were investigated by capillary GC using the chiral stationary phases Chirasil-L-Val, Chirasil-D-Val, and Lipodex E. Besides L-AA, in all bacteria D-amino acids (D-AA) were detected; those in the highest relative amounts were D-Ala and D-Asp (occurring in all bacteria) and, in several cases, D-Glu. Lower, but significant amounts of other D-AA such as D-Ser, D-Pro, D-Val, D-Thr, D-Ile, D-Leu, D-Met, D-Phe, D-Tyr, D-Orn, and D-Lys were also detected in certain bacteria. These findings explain the origin of D-AA found in all fermented foods and drinks produced with the aid of bacterial starter cultures. © 1993 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Fresenius' Zeitschrift für analytische Chemie 327 (1987), S. 32-32 
    ISSN: 1618-2650
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 0170-2041
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Synthese von L-Prolyl-leucyl-α-aminoisobutyryl-α-aminoisobutyryl-glutamyl-valinol und Identitätsbeweis mit dem isolierten C-terminalen Fragment von Trichotoxin A-40Die beiden hexapeptide L-Prolyl-L-leucyl-α-aminoisobutyryl-α-aminoisobutyryl-L-glutamyl-[oder L-glutaminyl-]L-valinol (7 and 8) wurden mittels Fragmentkondensation aus Z-L-Pro-Leu-Aib-Aib-OH (5a) und L-Glu(But)- Vol (9b) bzw. L-Gln-Vol (10) synthetisiert. Das synthetische Segment 7 erwies sich mit folgenden Methoden als identisch mit einem C-terminalen Fragment aus selektiv gespaltenem Trichotoxin A-40: Dünnschichtchromatographie, Aminosäurenanalyse, GC an chiraler Phase, Felddesorptionsmassenspektrometrie, 13C-NMR-Spektroskopie und Circulardichroismus. Die α-Verknüpfung des C-terminalen Aminoalkohols konnte durch selektive Trifluoracetolyse des natürlichen Pro-Leu-Aib-Aib[Iva]-Glu-Vol (7a and 7b) und des synthetischen Pro-Leu-Aib-Aib-Glu-Vol (7) sowie Vergleich mit synthetischem Glu-Vol (9), Gln-Vol (10), Glu(Vol) (11) und Glu(Vol)-NH2 (12) gezeigt werden. Ferner gelang es, die Kinetik der Valinol-Abspaltung durch wäßriges 6 N HCI/Dioxan anhand von Aminosäurenanalysen für das natürliche und synthetische Hexapeptid (7) aufzunehmen. Einschließlich des Aminosäureaustausches aufgrund der biosynthetischen Mikroheterogenität lautet somit die Primärstruktur von Trichotoxin A-40: Ac-Aib-Gly[L-Ala]-Aib-L-Leu-Aib-L-Gln-Aib-Aib-Aib-[L-Ala]-L-Ala-Aib-Aib-L-Pro-L-Leu-Aib-D-Iva[Aib]-L-Glu-L-Vol (1).
    Notes: The two hexapeptides L-prolyl-L-leucyl-α-aminoisobutyryl-α-aminoisobutyryl-L-glutamyl-[or L-glutaminyl-, respectively]L-valinol (7 and 8) were synthesized via fragment condensation of Z-L-Pro-L-Leu-Aib-Aib-OH (5a) with L-Glu(But)-Vol (9b) [or L-Gln-Vol (10), respectively]. The synthetic segment 7 was found to be identical with a C-terminal fragment isolated from selectively cleaved trichotoxin A-40 using thin layer chromatography, amino acid analysis, chiral phase gas chromatography, field desorption mass spectrometry, 13C NMR spectroscopy, and circular dichroism. The α-linkage of the C-terminal amino alcohol was shown via selective trifluoroacetolyses of natural Pro-Leu-Aib-Aib[Iva]-Glu-Vol (7a and 7b) and synthetic Pro-Leu-Aib-Aib-Glu-Vol (7) and comparison with synthetic Glu-Vol (9), Gln-Vol (10), Glu(Vol) (11), and Glu(Vol)-NH2 (12). Furthermore, the kinetics of the cleavage of valinol from both natural and synthetic hexapeptide (7) using 6 N HCI/dioxane was determined by quantitative amino acid analysis. Therefore, including amino acid exchanges due to biosynthetic microheterogeneity, the primary structure of trichotoxin A-40 is Ac-Aib-Gly[L-Ala]-Aib-L-Leu-Aib-L-Gln-Aib-Aib-Aib-[L-Ala]-L-Ala-Aib-Aib-L-Pro-L-Leu-Aib-D-Iva[Aib]-L-Glu-L-Vol (1).
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 9 (1982), S. 39-42 
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: By treatment with trifluoroacetic acid at 37°C the octadecapeptide antibiotic complex trichotoxin A 40 could be cleaved into three homologous N-acetylated dodecapeptides and two homologous pseudohexapeptides. After separation the peptides were converted to trimethylsilylated N-ethylpolyamino alcohols and investigated by capillary gas chromatography and mass spectrometry. Mass spectrometric analysis demonstrated the presence of a glutamine residue at position 6 and of a glutamic acid residue at position 17.
    Additional Material: 2 Ill.
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 4 (1998), S. 502-510 
    ISSN: 1075-2617
    Keywords: X-ray crystal structure ; gliodeliquescin ; alamethicin ; hypelcin ; paracelsin ; Ac, acetyl ; pBrBz, para-bromobenzoyl ; Me, methyl ; Piv, pivaloyl ; Z, benzyloxycarbonyl ; tBu, tert butyl ; TFA, trifluoroacetic acid ; EDCI, N-ethyl-N′-(3-dimethyl-aminopropyl)-carbodiimide HOBt, 1-hydroxybenzotriazole ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Ac-(Aib-Ala)3-OH (a protected segment of the peptaibols gliodeliquescin and paracelsin), Z-Leu-Aib-Val-Aib-Gly-OtBu (a segment of [Leu]7-gliodeliquescin), Z-Val-Aib-Aib-Gln-OtBu (a common segment of alamethicin, paracelsin, and hypelcin), and Ac-Aib-Pro-(Aib-Ala)2-OMe and Z-Aib-Pro-(Aib-Ala)2-OMe, which represent differently Nα-protected 1-6 segments of alamethicin and hypelcin, have been synthesized by solution methods. The crystal-state conformations of these five Aib-containing peptides have been determined by X-ray diffraction analysis. We have confirmed that the 310-helical structure is preferentially adopted by Aib-rich short peptides. An experimentally unambiguous proof for the 310→α-helix conversion has been provided by the two differently N-blocked -Aib-Pro-(Aib-Ala)2-OMe hexapeptides. The β-bend ribbon conformation, commonly observed in the (Aib-Pro)n sequential oligopeptides, is not found in the -Aib-Pro-Aib-Ala-Aib-Ala- sequence. As expected on the basis of the l-configuration of the Cα-monoalkylated residues, a right-handed helix screw sense was found in all peptides investigated. © 1998 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 2 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Journal of High Resolution Chromatography 23 (2000), S. 576-582 
    ISSN: 0935-6304
    Keywords: Gas chromatography-mass spectrometry ; amino acid enantiomers ; D-amino acids ; physiological fluids ; mammals ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: ---Quantities of D-amino acids were determined in body fluids (urine, blood plasma and blood serum, milk) of mammals (hamster, horse, bovine, sheep, pig, and dog). Amino acids were isolated using a cation exchanger and converted into their N(O)-pentafluoropropionyl (or trifluoroacetyl) amino acid 2-propyl esters. Enantiomers were separated and quantified on a Chirasil-L-Val capillary column with mass spectrometric detection using selected ion monitoring. D-Enantiomers of most protein L-amino acids were detected. Largest absolute and relative amounts in most cases were determined for D-Ser and D-Ala in urine. Stereoisomers of 2,6-diaminopimelic acid were also measured in bovine, ovine, and porcine urine. Since D-amino acids were detected in all representative classes of the major orders of Mammalia, namely Artiodactyla, Perissodactyla, Rodentia, and Carnivora, and taking reports in the literature into account, it is postulated that D-amino acids occur in all mammals.
    Additional Material: 5 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Liebigs Annalen 1997 (1997), S. 767-772 
    ISSN: 0947-3440
    Keywords: Peptide antibiotics ; Mycotoxins ; Peptaibols ; Peptaibiotics ; Sequence determination ; Mass spectrometry ; Non-proteinogenic amino acids ; α-Aminoisobutyric acid ; Isovaline ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: From a submerse culture of the fungus Hypocrea muroiana Hino et Katsumoto (Ascomycetes: Hypocreales) two major groups of peptides, designated hypomurocin (HM) A and B, belonging to the peptaibol family, could be characterized. Both groups showed antibiotic activity (Bacillus subtilis) and caused hemolysis of rat erythrocytes, HM A being less active than HM B. Peptides were isolated from the culture broth by chromatography on XAD-2 adsorber resin, octyl silica, and Sephadex LH 20. HM A and B were separated by preparative TLC, and individual peptides from each microheterogeneous group were isolated by preparative HPLC. Amino acid analysis and sequence determination by fast atom bombardment and electrospray tandem mass spectrometry revealed the composition and structures of six 11-mer peptides of the HM A group and of six 18-mer peptides of the HM B group. Positions of isomeric amino acids Leu/Ile and Val/Iva (present in some of the peptides) were determined by methanolytic cleavage of the pure peptides, followed by trifluoroacetylation of the dipeptide methyl esters released and assignment of their structures by gas chromatography-selected ion monitoring mass spectrometry. As examples, two sequences of HM A and HM B are presented (exchange positions in parentheses). - HM A-1(2): Ac-Aib1(D-Iva1)-Gln-Val-Val-Aib-Pro-Leu-Leu-Aib-Pro-Leuol11; HMB-1(2): Ac-Aib1-Ser-Ala-Leu-Aib-Gln-Aib-Val-Aib-Gly-Aib-Pro-Leu-Aib-Aib-Gln-Valol18 (Leuol18), (Ac = acetyl, Aib = α-aminoisobutyric acid, Iva = D-isovaline, Leuol = L-leucinol, Valol = L-valinol).
    Additional Material: 4 Ill.
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  • 10
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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