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Titolo:
The outstanding biological stability of beta- and gamma-peptides toward proteolytic enzymes: An in vitro investigation with fifteen peptidases
Autore:
Frackenpohl, J; Arvidsson, PI; Schreiber, JV; Seebach, D;
Indirizzi:
ETH Zurich, Organ Chem Lab, CH-8092 Zurich, Switzerland ETH Zurich Zurich Switzerland CH-8092 m Lab, CH-8092 Zurich, Switzerland
Titolo Testata:
CHEMBIOCHEM
fascicolo: 6, volume: 2, anno: 2001,
pagine: 445 - 455
SICI:
1439-4227(20010601)2:6<445:TOBSOB>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
HELICAL SECONDARY STRUCTURE; NMR-SOLUTION STRUCTURE; AMINO-ACIDS; SIDE-CHAINS; CD SPECTRA; HEXAPEPTIDE; ANALOGS; TETRAPEPTIDE; SUBSTRATE; METHANOL;
Keywords:
hydrolases; peptidases; peptides; peptidomimetics; proteolysis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
83
Recensione:
Indirizzi per estratti:
Indirizzo: Seebach, D ETH Zurich, Organ Chem Lab, Univ Str 16, CH-8092 Zurich, Switzerland ETH Zurich Univ Str 16 Zurich Switzerland CH-8092 Switzerland
Citazione:
J. Frackenpohl et al., "The outstanding biological stability of beta- and gamma-peptides toward proteolytic enzymes: An in vitro investigation with fifteen peptidases", CHEMBIOCHEM, 2(6), 2001, pp. 445-455

Abstract

A series of 36 linear and cyclic beta- and gamma -peptides consisting of as few as two, and as many as 15 residues, was offered as substrates to 15 commercially available proteases of bacterial, fungal and eukaryotic origin,including a beta -lactamase and amidases, as well as most vigorous, nonspecific proteases, such as the 20S proteasome from human erythrocytes. For comparison, an alpha -eicosapeptide and standard substrates of the proteolytic enzymes were included in the investigation. Under conditions of complete cleavage of the alpha -peptide within 15 min the beta- and gamma -peptides were stable for at least 48h. Inhibition studies with seven beta- and gamma-peptides and alpha -chymotrypsin that the residual enzyme activity towardsuccinyl-Ala-Ala-Pro-Phe-p-nitroanilide is unchanged within experimental error after incubation for 15min with the peptide analogues. Thus, beta- andgamma -peptides with proteinogenic side chains, that is, consisting of thesingly or doubly homologated natural alpha -amino acids (one or two CH2 groups inserted in the backbone of each residue) are completely stable to common proteases, without inhibiting their normal activity (as demonstrated for alpha -chymotrypsin). this proteolytic stability of peptides built of homologated amino acids is a prerequisite for their potential use as drugs.

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Documento generato il 05/07/20 alle ore 13:32:33