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Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

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[Spatial structure of Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH2 molecule].

Biofizika·2014
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[Spatial structure of isoleucine pentapeptides Glu-Phe-Leu-Arg-Ile-NH2 and Pro-Phe-Tyr-Arg-Ile-NH2].

Biofizika·2008
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[Spatial structure of BAM-12P dodecapeptide and its analogues].

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[Tertiary structure of myelopeptides. II. Conformational analysis of Phe-Arg-Pro-Arg-Ile-Met-Thr-Pro, Val-Val-Tyr-Pro-Asp, and Val-Asp-Pro-Pro].

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[Spatial structure of myelopeptides: I. Conformational analysis of MP-1, MP-2, and MP-3].

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[Spatial structure of the cardioactive octapeptide].

L I Ismailova, R M Abbasly, N A Akhmedov

    Biofizika
    |January 30, 2008
    PubMed
    Summary

    Theoretical conformational analysis revealed six stable low-energy structures for the cardioactive octapeptide, Pro-Gln-Asp-Pro-Phe-Leu-Arg-Ile-NH2. This peptide

    Area of Science:

    • Biochemistry and Molecular Biophysics
    • Computational Chemistry

    Context:

    • Understanding the three-dimensional structure of peptides is crucial for elucidating their biological function.
    • Cardioactive peptides play significant roles in cardiovascular regulation.
    • Theoretical conformational analysis provides a powerful tool for predicting peptide structures.

    Purpose:

    • To determine the low-energy spatial conformations of the cardioactive octapeptide Pro1-Gln2-Asp3-Pro4-Phe5-Leu6-Arg7-Ile8-NH2.
    • To analyze the dihedral angles and intra/interresidual interactions governing the peptide's structure.
    • To identify the stable structural forms of the octapeptide's main chain.

    Summary:

    • Theoretical conformational analysis was employed to investigate the spatial structure of the cardioactive octapeptide Pro-Gln-Asp-Pro-Phe-Leu-Arg-Ile-NH2.

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  • The study identified multiple low-energy conformations, detailing dihedral angles and interaction energies.
  • Six stable low-energy forms of the octapeptide's main chain were determined.

    • Impact:

    • Provides fundamental insights into the structural basis of cardioactive peptide function.
    • Contributes to the understanding of peptide folding and stability.
    • Informs future drug design and development targeting cardiovascular pathways.