Background: Inhibitors of chymase appear to be interesting compounds to develop drugs for the treatment of cardiovascular diseases. We used a computational approach to screen molecules from ZINC Biogenic Compounds database and to investigate their interactions with the enzyme, in order to predict their binding energy with respect to known ligands and to evaluate their selectivity. Results: Some screened compounds have a predicted binding energy comparable or even better with respect to that of known chymase inhibitors, and they interact with chymase key amino acids responsible for substrate selectivity. Moreover, these compounds appear to be more selective for chymase than to other serine proteases. Conclusion: These compounds are promising for the development of a new class of drugs for cardiovascular diseases. Pharmacophore model obtained for human chymase (PDB ID: 1T31).

In silico approach to find chymase inhibitors among biogenic compounds

FACCHIANO, Angelo
Methodology
;
MARABOTTI, ANNA
Supervision
2016-01-01

Abstract

Background: Inhibitors of chymase appear to be interesting compounds to develop drugs for the treatment of cardiovascular diseases. We used a computational approach to screen molecules from ZINC Biogenic Compounds database and to investigate their interactions with the enzyme, in order to predict their binding energy with respect to known ligands and to evaluate their selectivity. Results: Some screened compounds have a predicted binding energy comparable or even better with respect to that of known chymase inhibitors, and they interact with chymase key amino acids responsible for substrate selectivity. Moreover, these compounds appear to be more selective for chymase than to other serine proteases. Conclusion: These compounds are promising for the development of a new class of drugs for cardiovascular diseases. Pharmacophore model obtained for human chymase (PDB ID: 1T31).
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11386/4669138
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? 4
  • Scopus 22
  • ???jsp.display-item.citation.isi??? 22
social impact