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Related Experiment Videos

Structural requirements for formyl homooligopeptide chemoattractants.

C Toniolo, G M Bonora, H Showell

    Biochemistry
    |February 14, 1984
    PubMed
    Summary

    Researchers synthesized formylated homooligopeptides to study their effects on immune cells. The study found that longer peptides, specifically tetrapeptides and pentapeptides, showed the highest activity in stimulating white blood cell enzyme secretion.

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    Fibrils or globules? Tuning the morphology of peptide aggregates from helical building blocks.

    The journal of physical chemistry. B·2013

    Area of Science:

    • Medicinal Chemistry
    • Immunology
    • Biochemistry

    Background:

    • Chemotactic peptides, such as N-alpha-formylmethionylleucylphenylalanine, play a crucial role in neutrophil recruitment.
    • Understanding the structure-activity relationship of these peptides is essential for developing immunomodulatory agents.

    Purpose of the Study:

    • To synthesize and characterize N alpha-formylated homooligopeptides derived from L-methionine, L-norleucine, and S-methyl-L-cysteine.
    • To investigate the impact of peptide chain length and sulfur atom position on biological activity and conformation.
    • To correlate biological and conformational data with a proposed model of the chemotactic peptide receptor.

    Main Methods:

    • Solution peptide synthesis to create peptide series from dipeptides to heptapeptides.

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  • Biological assays measuring the induction of rabbit peritoneal polymorphonuclear leukocytes (PMNs) enzyme secretion in the presence of cytochalasin B.
  • Conformational analysis using infrared absorption and circular dichroism in various solvents (chloroform, TFE, HFIP, organic-aqueous mixtures).

    • Main Results:

    • The highest biological activity, measured by PMN enzyme secretion, was observed at the tetrapeptide and pentapeptide stages for the synthesized N alpha-formylated C-methoxy homooligopeptide series.
    • Conformational studies revealed tendencies for antiparallel-chain beta-associated and folded structures, influenced by solvent polarity.
    • The findings support the model that the formylpeptide receptor can accommodate peptides of at least four amino acid residues.

    Conclusions:

    • Peptide length is a critical factor in the biological activity of N alpha-formylated chemotactic peptides.
    • The presence and position of sulfur atoms, along with conformational preferences, modulate peptide function.
    • The study provides valuable insights into the molecular basis of formylpeptide receptor recognition and activation.