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Related Experiment Videos

Cyclic peptide substrates of pp60c-src. Synthesis and evaluation

J S McMurray1, R J Budde, D F Dyckes

  • 1Department of Neuro-Oncology, University of Texas M.D. Anderson Cancer Center, Houston.

International Journal of Peptide and Protein Research
|September 1, 1993
PubMed
Summary

Cyclic peptides were synthesized and tested against pp60c-src kinase. Inserting D-Phe-Pro altered kinetic parameters, showing higher Vmax but similar Km compared to linear substrates.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Medicinal Chemistry

Background:

  • pp60c-src is a proto-oncogene product implicated in cancer.
  • Understanding peptide substrate kinetics is crucial for drug development.
  • Cyclic peptides offer conformational constraints that can influence biological activity.

Purpose of the Study:

  • To investigate how constrained conformation and amino acid sequence affect peptide kinetic parameters.
  • To synthesize and evaluate cyclic peptides as substrates and inhibitors of pp60c-src.
  • To compare the kinetic properties of cyclic peptides with their linear counterparts.

Main Methods:

  • Solid-phase peptide synthesis (SPPS) using Fmoc chemistry.
  • Cleavage from resin and cyclization using BOP reagent.

Related Experiment Videos

  • Kinetic analysis of peptide substrates and inhibitors for pp60c-src activity.
  • Comparison with linear analogues and Val-5 angiotensin II.

    • Main Results:

    • Cyclization had minimal impact on the binding (Ki, Km) and phosphorylation rate (Vmax) of simple cyclic peptides.
    • Incorporation of a D-Phe-Pro dipeptide into cyclic decapeptides significantly altered kinetic parameters (Ki, Km, Vmax).
    • D-Phe-Pro containing cyclic peptides exhibited higher Vmax values than linear substrates, with comparable Km values in the millimolar range.

    Conclusions:

    • Constrained conformation via cyclization has a limited effect on pp60c-src kinetics for certain sequences.
    • Specific amino acid insertions, like D-Phe-Pro, can dramatically modulate peptide substrate efficiency.
    • These findings provide insights into the design of peptide-based modulators of pp60c-src activity.