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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
    Helix induction potential of N-terminal α-methyl, α-amino acids (1998)
    Springer
    International journal of peptide research and therapeutics 5 (1998), S. 105-107 
    Details
    ISSN: 1573-3904
    Keywords: α-aminoisobutyric acid peptides ; circular dichroism ; conformational analysis ; isovaline peptides ; C-peptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A series of longer analogues of the C-peptide of RNAse A has been synthesized with the aim of assessing the helix induction potential in water of α-methyl, α-amino acids at the N-terminus of the chain. The circular dichroism data indicate that one isovaline residue is effective in increasing the helix content of the 13-residue peptide by about 7%.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008873910529
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  • 4
    Electronic Resource
    Electronic Resource
    Helix induction potential of N-terminal α-methyl, α-amino acids (1998)
    Springer
    International journal of peptide research and therapeutics 5 (1998), S. 105-107 
    Details
    ISSN: 1573-3904
    Keywords: α-aminoisobutyric acid peptides ; circular dichroism ; conformational analysis ; isovaline peptides ; C-peptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary A series of longer analogues of the C-peptide of RNAse A has been synthesized with the aim of assessing the helix induction potential in water of α-methyl, α-amino acids at the N-terminus of the chain. The circular dichroism data indicate that one isovaline residue is effective in increasing the helix content of the 13-residue peptide by about 7%.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443448
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  • 5
    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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  • 6
    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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  • 7
    Electronic Resource
    Electronic Resource
    Conformation and membrane activity of an analogue of the peptaibol antibiotic trichogin GA IV with a lipophilic amino acid at the N-terminus (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 4 (1998), S. 389-399 
    Details
    ISSN: 1075-2617
    Keywords: conformational analysis ; lipo-amino acid ; membrane activity ; NMR ; peptide antibiotic ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: We have synthesized by solution-phase methods two analogues of the 11-residue lipopeptaibol antibiotic trichogin GA IV in which the N-terminal n-octanoyl group is replaced either by an N-acetylated 2-amino-2-methyl-l-undecanoic acid or by an N-acetylated α-aminoisobutyric acid. CD, FTIR absorption, and NMR analyses unequivocally show that the main structural features of trichogin GA IV are preserved in these analogues. Since only the peptide containing the lipophilic chain exhibits membrane-modifying properties, these results strongly support the view that moving the long acyl moiety from the Nα-blocking group to the side chain of the N-terminal extra-residue does not affect the conformational properties or the membrane activity of trichogin GA IV. © 1998 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 5 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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