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Conformational transitions of leucine-containing isomeric sequential basic polytripeptides.

S Stokrová, M Bohdanecký, K Bláha

    Biopolymers
    |October 1, 1989
    PubMed
    Summary

    Polypeptides containing lysine or arginine residues undergo conformational changes in salt solutions. Arginine-based polypeptides show high helical stability with minimal aggregation, unlike lysine-based ones.

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    Area of Science:

    • Biochemistry
    • Polymer Science
    • Structural Biology

    Background:

    • Sequential polytripeptides are model systems for studying protein folding.
    • Hydrophobic interactions and charge effects influence polypeptide conformation and aggregation.

    Purpose of the Study:

    • To investigate conformational transitions in basic sequential polytripeptides.
    • To compare the behavior of lysine- and arginine-containing polypeptides under varying conditions.

    Main Methods:

    • Circular Dichroism (CD) spectroscopy to assess secondary structure.
    • Sedimentation equilibrium and viscometry to study aggregation and molecular weight.

    Main Results:

    • Lysine-containing polypeptides (Lys-Ala-Leu)n and (Lys-Leu-Ala)n exhibit high helicity and aggregate in high salt solutions.

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  • Arginine-containing polypeptides (Arg-Ala-Ala)n, (Arg-Leu-Ala)n, and (Arg-Ala-Leu)n adopt alpha-helical conformations with significantly lower aggregation tendencies.
  • Hydrophobic interactions between lysine and leucine residues impact helix stabilization and aggregation differently based on sequence.

    • Conclusions:

    • Polypeptide sequence and amino acid composition dictate conformational stability and aggregation behavior.
    • Arginine residues promote alpha-helical formation with reduced aggregation compared to lysine residues in these model systems.