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  • 1
    Electronic Resource
    Electronic Resource
    Afc can adopt either the fully extended or a turn conformation (2000)
    Springer
    International journal of peptide research and therapeutics 7 (2000), S. 123-131 
    Details
    ISSN: 1573-3904
    Keywords: 9-amino-9-fluorenecarboxylic acid ; conformational analysis ; fluorescence ; peptide synthesis ; X-ray diffraction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract We have synthesized by solution methods and fully characterizedtwo sets of terminally protected peptides based on the tricyclic Cα α-disubstituted glycine Afc. Theconformational preferences of the Afc/Gly peptides were examined by FT-IR absorption and 1H NMR techniques, whilethose of the Afc/TOAC peptides were primarily investigated by using fluorescence spectroscopy. The X-ray diffraction structure of an Afc derivative was also analyzed. The body of solution and crystal-state experimental data conclusively confirms previous findings that the Afc residue may either adopt the fully extended (C5) or a turn conformation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008915732443
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  • 2
    Electronic Resource
    Electronic Resource
    Afc can adopt either the fully extended or a turn conformation (2000)
    Springer
    International journal of peptide research and therapeutics 7 (2000), S. 123-131 
    Details
    ISSN: 1573-3904
    Keywords: 9-amino-9-fluorenecarboxylic acid ; conformational analysis ; fluorescence ; peptide synthesis ; X-ray diffraction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary We have synthesized by solution methods and fully characterized two sets of terminally protected peptides based on the tricyclic Cα,α-disubstituted glycine Afc. The conformational preferences of the Afc/Gly peptides were examined by FT-IR absorption and1H NMR techniques, while those of the Afc/TOAC peptides were primarily investigated by using fluorescence spectroscopy. The X-ray diffraction structure of an Afc derivative was also analyzed. The body of solution and crystal-state experimental data conclusively confirms previous findings that the Afc residue may either adopt the fully extended (C5) or a turn conformation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443571
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  • 3
    Electronic Resource
    Electronic Resource
    Crystallographic structure of a helical lipopeptaibol antibiotic analogue (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 213-218 
    Details
    ISSN: 1573-3904
    Keywords: α/310-Helix〉 ; Nitroxide amino acid ; Peptide conformation ; X-ray diffraction ; α-Tetrasubstituted amino acids ; Trichogin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract An X-ray diffraction analysis of the [Fmoc0,TOAC4,8, Leu-OMe11] analogue of thelipopeptaibol antibiotic trichogin A IV shows that the undecapeptide isfolded in a right-handed, mixed α/310-helix. The helicalmolecules are connected in a head-to-tail arrangement along the b-axisthrough C=O···H-N intermolecular H-bonding. Thispacking mode generates a hydrophobic cavity where the FmocNα-protecting groups are accommodated. The distances andangles between the nitroxide groups of the two TOAC residues, separated byone turn of the α-helix, have been determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008874816982
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  • 4
    Electronic Resource
    Electronic Resource
    The polypeptide 310-helix as a template and a spacer (1995)
    Springer
    International journal of peptide research and therapeutics 2 (1995), S. 187-189 
    Details
    ISSN: 1573-3904
    Keywords: β-turns ; Cα-tetrasubstituted α-amino acids ; Conformational restrictions ; Peptide conformation ; X-ray diffraction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary X-ray diffraction analyses have provided detailed structural information on the 310-helices of (i) pBrBz-d-(αMe)Phe-(Aib)2-d-(αMe)Phe-Aib-OtBu and Ac-(Aib)2-l-Lys(Bz)-(Aib)2-l-Lys(Bz)-(Aib)2-NHMe as suitable templates for molecular recognition studies, and (ii) pBrBz-TOAC-(l-Ala)2-TOAC-l-Ala-NHtBu as an appropriate spacer for an ESR study of side chain to side chain interactions. In addition, in Ac-TOAC-(Aib)2-l-Trp-Aib-OMe, forming a 310-helix, the TOAC residue plays the role of an effective quencher of the fluorescence of the tryptophan residue located one turn apart.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00119149
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  • 5
    Electronic Resource
    Electronic Resource
    Crystallographic structure of a helical lipopeptaibol antibiotic analogue (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 213-218 
    Details
    ISSN: 1573-3904
    Keywords: α/310-Helix ; Nitroxide amino acid ; Peptide conformation ; X-ray diffraction ; α-Tetrasubstituted amino acids ; Trichogin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary An X-ray diffraction analysis of the [Fmoc0, TOAC4,8, Leu-OMe11]analogue of the lipopeptaibol antibiotic trichogin A Iv shows that the undecapeptide is folded in a right-handed, mixed α/310-helix. The helical molecules are connected in a head-to-tail arrangement along the b-axis through C=O...H-N intermolecular H-bonding. This packing mode generates a hydrophobic cavity where the Fmoc Nα-protecting groups are accommodated. The distances and angles between the nitroxide groups of the two TOAC residues, separated by one turn of the α-helix, have been determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02442878
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  • 6
    Electronic Resource
    Electronic Resource
    Conformational Characterization of the 1-Aminocyclobutane-1-carboxylic Acid Residue in Model Peptides (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 3 (1997), S. 110-122 
    Details
    ISSN: 1075-2617
    Keywords: β-bend ; cyclic amino acid ; 310-helix ; peptide conformation ; X-ray diffraction ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A series of N- and C-protected, monodispersed homo-oligopeptides (to the dodecamer level) from the small-ring alicyclic Cα,α-dialkylated glycine 1-aminocyclobutane-1-carboxylic acid (Ac4c) and two Ala/Ac4c tripeptides were synthesized by solution methods and fully characterized. The conformational preferences of all the model peptides were determined in deuterochloroform solution by FT-IR absorption and 1H-NMR. The molecular structures of the amino acid derivatives Z-Ac4c-OH and Z2-Ac4c-OH, the tripeptides Z-(Ac4c)3-OtBu, Z-Ac4c-(L-Ala)2-OMe and Z-L-Ala-Ac4c-L-Ala-OMe, and the tetrapeptide Z-(Ac4c)4-OtBu were determined in the crystal state by X-ray diffraction. The average geometry of the cyclobutyl moiety of the Ac4c residue was assessed and the τ(N-Cα-C′) bond angle was found to be significantly expanded from the regular tetrahedral value. The conformational data are strongly in favour of the conclusion that the Ac4c residue is an effective β-turn and helix former. A comparison with the structural propensities of α-aminoisobutyric acid, the prototype of Cα,α-dialkylated glycines, and the other extensively investigated members of the family of 1-aminocycloalkane-1-carboxylic acids (Acnc, with n=3, 5-8) is made and the implications for the use of the Ac4c residue in conformationally constrained peptide analogues are briefly examined. © 1997 European Peptide Society and John Wiley & Sons, Ltd
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Conformational characterization of peptides rich in the cycloaliphatic Cα,α-disubstituted glycine 1-amino-cyclononane-1-carboxylic acid (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 3 (1997), S. 367-382 
    Details
    ISSN: 1075-2617
    Keywords: β-turn ; cyclic amino acid ; 310-helix ; peptide conformation ; X-ray diffraction ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A series of N- and C-protected, monodispersed homo-oligopeptides (to the pentamer level) from the cycloaliphatic Cα,α,-dialkylated glycine 1-aminocyclononane-1-carboxylic acid (Ac9c) and two Ala/Ac9c tripeptides have been synthesized by solution methods and fully characterized. The conformational preferences of all the model peptides were determined in deuterochloroform solution by FT-IR absorption and 1H-NMR. The molecular structures of the amino acid derivatives mClAc-Ac9c-OH and Z-Ac9c-OtBu, the dipeptide pBrBz-(Ac9c)2-OtBu, the tetrapeptide Z-(Ac9c)4-OtBu, and the pentapeptide Z-( Ac9c)5-OtBu were determined in the crystal state by X-ray diffraction. Based on this information, the average geometry and the preferred conformation for the cyclononyl moiety of the Ac9c residue have been assessed. The backbone conformational data are strongly in favour of the conclusion that the Ac9c residue is a strong β-turn and helix former. A comparison with the structural propensity of α-aminoisobutyric acid, the prototype of Cα,α-dialkylated glycines, and the other extensively investigated members of the family of 1-aminocycloalkane-1-carboxylic acids (Acnc, with n=3-8) is made and the implications for the use of the Ac9c residue in conformationally constrained analogues of bioactive peptides are briefly examined. © 1997 European Peptide Society and John Wiley & Sons, Ltd.J. Pep. Sci. 3: 367-382No. of Figures: 10. No. of Tables: 6. No. of References: 62
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Preferred conformation of peptides rich in Ac8c, a medium-ring alicyclic Cα,α-disubstituted glycine (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 2 (1996), S. 14-27 
    Details
    ISSN: 1075-2617
    Keywords: β-bend ; cyclic amino acid ; 310-helix ; peptide conformation ; X-ray diffraction ; Chemistry ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A complete series of terminally blocked, monodispersed homo-oligopeptides (to the pentamer level) from the sterically demanding, medium-ring alicyclic Cα,α-disubstituted glycine 1-aminocyclooctane-1-carb oxylic acid (Ac8c), and two Ala/Ac8c tripeptides, were synthesized by solution methods and fully characterized. The preferred conformation of all the oligopeptides was determined in deuterochloroform solution by IR absorption and 1H-NMR. The molecular structures of the amino acid derivative Z-Ac8c-OH, the dipeptide pBrBz- (Ac8c)2-OH and the tripeptide pBrBz-(Ac8c)3-OtBu were assessed in the crystal state by X-ray diffraction. Conformational energy computations were performed on the monopeptide Ac-Ac8c-NHMe. Taken together, the results obtained strongly support the view that the Ac8c residue is an effective β-turn and helix former. A comparison is also made with the conformational preferences of α-aminoisobutyric acid, the prototype of Cα, α-disubstituted glycines, and of the other members of the family of 1-aminocycloalkane-1-carboxylic acids (Acnc, with n=3, 5-7) investigated so far. The implications for the use of the Ac8c residue in peptide conformational design are considered.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.43
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