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Titolo:
NMR ANALYSIS OF THE ULTRAVIOLET PHOTOLYTIC BEHAVIOR OF SEVERAL TRYPTOPHAN-RICH GROWTH-HORMONE RELEASING PEPTIDES
Autore:
MCKIM S; HINTON JF; DEGHENGHI R;
Indirizzi:
SOUTHEASTERN OKLAHOMA STATE UNIV,DEPT PHYS SCI DURANT OK 74701 UNIV ARKANSAS,DEPT CHEM & BIOCHEM FAYETTEVILLE AR 72701 EUROPEPTIDES F-95100 ARGENTEUIL FRANCE
Titolo Testata:
Biospectroscopy
fascicolo: 4, volume: 3, anno: 1997,
pagine: 317 - 323
SICI:
1075-4261(1997)3:4<317:NAOTUP>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLANAR LIPID-MEMBRANES; GRAMICIDIN-A; RADIATION INACTIVATION; AQUEOUS-SOLUTIONS; INVIVO ACTIVITY; INVITRO; PITUITARY; RESIDUES; TUMOR; DIPEPTIDES;
Keywords:
GROWTH HORMONE RELEASING PEPTIDE; TRYPTOPHAN; 2-METHYL TRYPTOPHAN; GHRP-6; HEXARELIN; EP7458; ULTRAVIOLET PHOTOLYTIC DEGRADATION; RATE CONSTANTS; DIFFERENTIAL PHOTOLYSIS; PHOTOLYSIS PRODUCTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
S. Mckim et al., "NMR ANALYSIS OF THE ULTRAVIOLET PHOTOLYTIC BEHAVIOR OF SEVERAL TRYPTOPHAN-RICH GROWTH-HORMONE RELEASING PEPTIDES", Biospectroscopy, 3(4), 1997, pp. 317-323

Abstract

Aqueous solutions of three tryptophan-rich growth hormone releasing hexapeptides, GHRP-6 ( His-D-Trp-Ala-Trp-D-Phe-Lys-NH2), hexarelin (His-D-2-Me-Trp-Ala-Trp-D-Phe-Lys-NH2 ), and EP7458 ( His-D-Trp-Ala-2-Me-Trp-D-Phe-Lys-NH2), were exposed to varying durations of ultraviolet (UV) light. Using NMR spectroscopy, first-order rate constants for the UV photolytic degradation of the tryptophan(s)/2-methyl tryptophan residues within each peptide were obtained by plotting the decrease in thearea of the indole N-H resonances with respect to UV photolysis time. A significant differential photolytic effect was observed between thetwo tryptophan residues of GHRP-6 and the tryptophan/2-methyl tryptophan residues of EP7458. A somewhat smaller differential photolytic effect was observed between the tryptophan/2-methyl tryptophan residues of hexarelin. In addition, the three peptides were degraded at different rates, suggesting that the effect of UV light on each peptide is dependent on whether a tryptophan or 2-methyl tryptophan is the second orfourth residue in the primary sequence. (C) 1997 John Wiley & Sons, Inc.

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Documento generato il 09/07/20 alle ore 17:33:38