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Titolo:
Synthesis and antibacterial properties of peptidyl derivatives and cyclopeptides structurally based upon the inhibitory centre of human cystatin C - Dissociation of antiproteolytic and antibacterial effects
Autore:
Kasprzykowski, F; Schalen, C; Kasprzykowska, R; Jastrzebska, B; Grubb, A;
Indirizzi:
Univ Lund Hosp, Dept Clin Chem, S-22185 Lund, Sweden Univ Lund Hosp LundSweden S-22185 Dept Clin Chem, S-22185 Lund, Sweden Univ Lund Hosp, Dept Infect Dis & Med Microbiol, S-22185 Lund, Sweden UnivLund Hosp Lund Sweden S-22185 & Med Microbiol, S-22185 Lund, Sweden Univ Gdansk, Dept Chem, PL-80952 Gdansk, Poland Univ Gdansk Gdansk Poland PL-80952 k, Dept Chem, PL-80952 Gdansk, Poland
Titolo Testata:
APMIS
fascicolo: 7-8, volume: 108, anno: 2000,
pagine: 473 - 481
SICI:
0903-4641(200007/08)108:7-8<473:SAAPOP>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYSTEINE PROTEINASE-INHIBITORS; HERPES-SIMPLEX VIRUS; PORPHYROMONAS-GINGIVALIS; CHICKEN CYSTATIN; REPLICATION; GROWTH; CELLS; ALPHA;
Keywords:
antibacterial peptides; cystatin C; staphylococci; streptococci;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
18
Recensione:
Indirizzi per estratti:
Indirizzo: Grubb, A Univ Lund Hosp, Dept Clin Chem, S-22185 Lund, Sweden Univ Lund Hosp Lund Sweden S-22185 n Chem, S-22185 Lund, Sweden
Citazione:
F. Kasprzykowski et al., "Synthesis and antibacterial properties of peptidyl derivatives and cyclopeptides structurally based upon the inhibitory centre of human cystatin C - Dissociation of antiproteolytic and antibacterial effects", APMIS, 108(7-8), 2000, pp. 473-481

Abstract

Cysteine protease-inhibiting proteins of the cystatin superfamily can inhibit the replication of certain viruses and bacteria. The inhibitory centre of human cystatin C, the most widely distributed human cystatin, comprises three peptide segments. The present work describes the synthesis and antibacterial activity of 27 new peptidyl derivatives or cyclopeptides based uponthe aminoterminal segment Arg(8)-Leu(9)-Val(10)-Gly(11). Fourteen of the new compounds displayed antibacterial activity against from 1 up to 9 of 17 clinically important bacterial species tested. Antiproteolytic activity of a compound was usually not required for its antibacterial capacity. Peptidyl diazomethanes generally had a very narrow antibacterial spectrum, inhibiting only Streptococcus pyogenes, whereas cyclopeptides and peptidyl derivatives of the general structure X-Arg-Leu-NH-CH(iPr)-CH2-NH-Y had a much wider spectrum. The most potent of these substances displayed approximately equal minimal inhibitory and bactericidal concentrations of about 20 mug/ml for both Staphylococcus aureus and S. pyogenes and were devoid of antiproteolytic activity. Several of the new substances could protect mice against lethal intraperitoneal challenge with S. pyogenes. Though their target remainsto be disclosed, the group of substances here reported might be promising for the development of antibacterial drugs and the discovery of novel principles of action.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 12:08:15