Synthesis and biological activities of beta-chain fragments of hemoglobin / 药学学报
Acta Pharmaceutica Sinica
; (12): 1270-1274, 2010.
Article
em Zh
| WPRIM
| ID: wpr-354517
Biblioteca responsável:
WPRO
ABSTRACT
To investigate the angiotensin I-converting enzyme (ACE) inhibitory activity of beta-chain hemoglobin fragments, 17 fragments were synthesized by microwave-assisted solid-phase synthesis method. Wang resin or Trt(2-Cl) resin, Fmoc and HBTU-HOBt were used as solid carrier, N-terminal amino acid protecting groups and coupling reagents, respectively. The ACE inhibitory, alpha-glucosidase inhibitory, antibacterial and antitumor activities of the synthesized fragments were assayed. In vitro, Val-Val-Tyr-Pro-Trp-Thr showed high ACE inhibitory activity (IC50 = 7.42 micromol x L(-1)). The results indicate that there are two active sites in Val-Val-Tyr-Pro-Trp-Thr-Gln-Arg-Phe, one consists of Val-Val-, and the other -Gln-Arg-Phe. Peptides showed high ACE inhibitory activity when the N-terminal was hydrophobic amino acid such as Val and C-terminal tripeptide contained Phe, Trp or Arg. Some of the fragments showed low a-glucosidase inhibitory activity. No antibacterial activity or antitumor activity was detected in vitro. The results indicate that these peptides have a potential antihypertensive effect and possible application in the treatment of hypertension.
Texto completo:
1
Índice:
WPRIM
Assunto principal:
Fragmentos de Peptídeos
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Farmacologia
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Inibidores da Enzima Conversora de Angiotensina
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Química
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Sequência de Aminoácidos
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Peptidil Dipeptidase A
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Linhagem Celular Tumoral
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Alfa-Glucosidases
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Globinas beta
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Técnicas de Síntese em Fase Sólida
Limite:
Humans
Idioma:
Zh
Revista:
Acta Pharmaceutica Sinica
Ano de publicação:
2010
Tipo de documento:
Article