Letters in Peptide Science

, Volume 2, Issue 3, pp 259–260

Screening of a synthetic pentapeptide library composed of d-amino acids against fructose-1,6-biphosphate aldolase

Authors

  • Isabelle Samson
    • Laboratory of Medicinal Chemistry (F.F.W.), Rega Institute for Medical ResearchKatholieke Universiteit Leuven
  • Jef Rozenski
    • Laboratory of Medicinal Chemistry (F.F.W.), Rega Institute for Medical ResearchKatholieke Universiteit Leuven
  • Arthur van Aerschot
    • Laboratory of Medicinal Chemistry (F.F.W.), Rega Institute for Medical ResearchKatholieke Universiteit Leuven
  • Bart Samyn
    • Department of Biochemistry, Physiology and MicrobiologyRijks Universiteit Gent
  • Jozel van Beeumen
    • Department of Biochemistry, Physiology and MicrobiologyRijks Universiteit Gent
  • Piet Herdewijn
    • Laboratory of Medicinal Chemistry (F.F.W.), Rega Institute for Medical ResearchKatholieke Universiteit Leuven
Section II. Synthesis and Libraries

DOI: 10.1007/BF00119166

Cite this article as:
Samson, I., Rozenski, J., van Aerschot, A. et al. Lett Pept Sci (1995) 2: 259. doi:10.1007/BF00119166

Summary

A synthetic peptide library, theoretically composed of 537 824 d-amino acid pentapeptides anchored on polystyrene beads, was prepared with each bead bearing a single pentapeptide sequence. This library was screened for interaction with fructose-1,6-biphosphate aldolase of T. brucei labelled with biotin. Affinity beads that bound the enzyme were selected with streptavidin-coated magnetic beads. A total of 19 beads were isolated and individually subjected to Edman microsequence analysis. The corresponding peptide sequences were synthesized and evaluated for enzyme activity inhibition.

Keywords

d-amino acidsLibraryAldolaseScreeningMagnetic beads
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Copyright information

© ESCOM Science Publishers B.V 1995