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Related Experiment Videos

Conformationally constrained D,L-alternating oligopeptides.

E Fenude, L Tomasic, G P Lorenzi

    Biopolymers
    |January 1, 1989
    PubMed
    Summary

    N-methyl groups in D,L-alternating peptides constrain beta-helical structures. This study shows N-methylation significantly alters peptide conformations, favoring specific beta-helices with maximal interchain hydrogen bonds.

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    Conformation and structure of linear peptides with regularly alternating L- and D-residues: structure of the blocked hexapeptide tert-butyloxycarbonyl-(D-alloisoleucyl-L-isoleucyl)3 methyl ester monohydrate.

    International journal of peptide and protein research·1995

    Area of Science:

    • Peptide Chemistry
    • Structural Biology
    • Organic Chemistry

    Background:

    • D,L-alternating peptides can form various beta-helical structures.
    • Conformational constraints are crucial for controlling peptide secondary structures.

    Purpose of the Study:

    • To investigate the effect of N-methylation as a conformational constraint on beta-helical structures in D,L-alternating peptides.
    • To analyze the structural behavior of specific N-methylated peptides.

    Main Methods:

    • Synthesis and characterization of N-methylated D,L-alternating peptides.
    • 1H-NMR spectroscopy to determine peptide conformations in chloroform.
    • Analysis of secondary structures formed, focusing on beta-helices.

    Main Results:

    • N-methylation at specific positions (n-3 or n-4) drastically alters peptide behavior compared to non-methylated analogues.
    • Peptides Boc(L-Nle-D-Nle)3-L-Nle-D-MeNle-L-Nle-D-Nle-L-Nle-OMe and its formyl analogue predominantly form beta 7.2-helices.
    • Peptide Boc(D-Leu-L-Leu)5-D-MeLeu-(L-Leu-D-Leu)2-OMe exclusively forms beta 5.6 or beta 7.2-helices.
    • All observed helices exhibit the maximum possible number of interchain hydrogen bonds.

    Conclusions:

    • N-methylation is an effective strategy to selectively reduce and control beta-helical structures in D,L-alternating peptides.
    • The position of the N-methyl group influences the specific type of beta-helix formed.
    • These findings contribute to the understanding of peptide folding and design principles.

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