Studies on analogs of a peptide derived from alpha-fetoprotein having antigrowth properties

L. E. Eisele, D. D. Vakharia, R. MacColl, G. J. Mizejewski, F. B. Mesfin, J. A. Bennett, T. T. Andersen, H. I. Jacobson

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


A 34-amino acid portion of the third domain of alpha-fetoprotein possesses antigrowth and anticancer activities. Three analogs of this sequence were chemically synthesized, in which the two cysteines of the original sequence were replaced by alanines, glycines or serines. The original cysteine and alanine peptides formed trimers at 0.20 g/L in pH 7.4 phosphate buffer, and the glycine and serine peptides formed dimers. Trimer preparations were more potent in inhibiting estrogen-induced growth in the mouse uterine assays than the two dimeric oligomers. Of salient importance is that the alanine peptide retained its trimeric form in solution much longer than the cysteine peptide. Antigrowth assays were performed starting with stock solutions at a peptide concentration of 0.20 g/L, because at very high peptide concentration (8.0 g/L) the peptides aggregated extensively. All the peptides, although differing in biological activity, had almost identical secondary structures. Unlike alpha-fetoprotein, the three peptides have low amounts of α-helix. Trifluoroethanol has the ability to convert peptides into a helical conformation when they have a propensity for that structure. At trifluoroethanol concentrations of 20% and higher, the alanine and glycine peptides were changed into highly helical structures.

Original languageEnglish (US)
Pages (from-to)539-546
Number of pages8
JournalJournal of Peptide Research
Issue number6
StatePublished - 2001
Externally publishedYes


  • Antigrowth peptides
  • Breast cancer treatments
  • Peptide conformation
  • Peptide oligomers
  • Transformed alpha-fetoprotein
  • Trifluoroethanol

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology


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