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Titolo:
Studies on a growth-inhibitory peptide derived from alpha-fetoprotein and some analogs
Autore:
Eisele, LE; Mesfin, FB; Bennett, JA; Andersen, TT; Jacobson, HI; Soldwedel, H; MacColl, R; Mizejewski, GJ;
Indirizzi:
New York State Dept Hlth, Wadsworth Ctr, Albany, NY 12201 USA New York State Dept Hlth Albany NY USA 12201 th Ctr, Albany, NY 12201 USA Albany Med Coll, Albany, NY 12208 USA Albany Med Coll Albany NY USA 12208Albany Med Coll, Albany, NY 12208 USA
Titolo Testata:
JOURNAL OF PEPTIDE RESEARCH
fascicolo: 1, volume: 57, anno: 2001,
pagine: 29 - 38
SICI:
1397-002X(200101)57:1<29:SOAGPD>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
BREAST-CANCER; FATTY-ACIDS; SERUM; STIMULATION; ESTRADIOL; RISK;
Keywords:
alpha-fetoprotein; alpha-fetoprotein peptides; anticancer peptides; breast cancer studies; disulfide bonds; estrogen-dependent mouse uterus growth; neoepitopes; peptide aggregation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Mizejewski, GJ New York State Dept Hlth, Wadsworth Ctr, POB 509, Albany, NY 12201 USA New York State Dept Hlth POB 509 Albany NY USA 12201 01 USA
Citazione:
L.E. Eisele et al., "Studies on a growth-inhibitory peptide derived from alpha-fetoprotein and some analogs", J PEPT RES, 57(1), 2001, pp. 29-38

Abstract

A 34-amino acid synthetic peptide was derived from the third domain of human alpha-fetoprotein, and the peptide was shown to inhibit estrogen-stimulated growth. Under certain conditions, however, the peptide lost growth-inhibitory activity. A biophysical study of the peptide was undertaken with a goal of obtaining completely reliable preparations. The peptide was studied using gel-filtration column chromatography as a function of peptide concentration and age of solution, and was found to exhibit complex aggregation behaviors. During the early period (0-3 h) after dissolving lyophilized peptide into pH 7.4 buffer, solutions were composed mostly of trimers. At higherpeptide concentrations (greater than or equal to3.0 g/L), the trimers aggregated extensively to a large aggregate (minimum size approximate to 102 peptides). At 5.0-8.0 g/L, these large aggregates increased in size (up to approximate to 146 peptides) until trimers were largely exhausted from solution. During the later times (>3 h) after sample preparation, the trimeric oligomer of the peptide dissociated slowly to form dimers for samples at 0.10-3.0 g/L. After their build-up, a very small number of dimers associated toform hexamers. Disulfide bonds stabilized the dimers as indicated by the conversion of dimers to trimers upon the addition of a reducing agent, and the failure of dimers to form in the presence of reducing agent. Reducing agent did not affect trimer or large aggregate formation. Trimers were found to be active in an assay monitoring inhibition of estrogen-stimulated growth, whereas dimers and large aggregates were inactive. The two cysteines in the peptide were modified to either S-methylcysteine or S-(2-aminoethyl)cysteine, and both derivatives showed significant growth-inhibition activity. A serine analog in which both cysteines were replaced had very different aggregation behavior than the cysteine peptide and lacked its growth inhibitory ability. Peptide aggregation is critically important in establishing theability of the peptide to inhibit growth and have anticancer activity, butthe state of its two cysteines is of little influence.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 22:00:02