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Related Experiment Videos

Structure-activity studies of vasoactive intestinal polypeptide.

M O'Donnell1, R J Garippa, N C O'Neill

  • 1Department of Pharmacology, Hoffmann-La Roche, Inc., Nutley, New Jersey 07110.

The Journal of Biological Chemistry
|April 5, 1991
PubMed
Summary

Vasoactive intestinal peptide (VIP) requires specific side-chain functional groups for receptor interaction. Identifying these key amino acid positions enhances VIP

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Area of Science:

  • Pharmacology
  • Molecular Biology
  • Neuropeptide Research

Background:

  • Vasoactive intestinal peptide (VIP) is a bronchodilator neuropeptide.
  • VIP's biological activity and receptor binding are sensitive to terminal residue modifications.
  • The entire primary sequence of VIP appears crucial for VIP receptor recognition.

Purpose of the Study:

  • To identify critical side-chain functional groups in VIP necessary for receptor interaction.
  • To probe the VIP pharmacophore using alanine substitution.
  • To understand structure-activity relationships for enhancing VIP's potency.

Main Methods:

  • Alanine scanning mutagenesis of the VIP molecule.
  • In vitro receptor binding affinity assays.

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  • In vivo biological potency assessments.

    • Main Results:

    • VIP's full primary sequence is necessary for receptor binding.
    • Specific residues (Asp3, Phe6, Thr7, Tyr10, Tyr22, Leu23) are key components of the VIP pharmacophore.
    • The VIP pharmacophore is conserved between guinea pig and human lung.

    Conclusions:

    • Multiple binding sites within the VIP primary sequence are essential for receptor interaction.
    • Targeting these identified positions can optimize VIP's binding energy.
    • This knowledge can guide the development of more potent VIP-based therapeutics.