SciELO - Scientific Electronic Library Online

 
vol.66Natural products research in South Africa: End of an era on land or the beginning of an endless opportunity in the sea?Synthesis, spectroscopic and pharmacological studies of bivalent copper, zinc and mercury complexes of thiourea índice de autoresíndice de assuntospesquisa de artigos
Home Pagelista alfabética de periódicos  

Serviços Personalizados

Artigo

Indicadores

Links relacionados

  • Em processo de indexaçãoCitado por Google
  • Em processo de indexaçãoSimilares em Google

Compartilhar


South African Journal of Chemistry

versão On-line ISSN 1996-840X
versão impressa ISSN 0379-4350

Resumo

SINGH, Parvesh. Conformational preferences of Amphibian peptides Brevinin-Ya and Brevinin-Yb explored using molecular dynamics. S.Afr.j.chem. (Online) [online]. 2013, vol.66, pp.00-00. ISSN 1996-840X.

The brevinin-1 family peptides obtained from different frog skins have great potency against bacterial and fungal infections. Their biological activities are significantly affected by mutations especially at positions 11 and 14. However, despite having great medicinal potential, the detailed information regarding their three-dimensional structures is still not fully known. In the present study, the conformational profiles of two brevinin peptides (Brevinin 1-Ya and Brevinin 1-Yb) were explored at molecular mechanics level using molecular dynamics (MD) method. Specifically, four MD simulations (Brev1_Ya(E), Brev1_Yb(E), Brev1_Ya(H), Brev1_Yb(H)) were performed starting from extended as well as helical conformations of both peptides under implicit solvent conditions. The analysis of the results indicated that both peptides have a strong tendency to attain α-helical character, preferably from their central residues extending towards their C-terminals12-23, whereas their N-terminal residues stay either in β-turn or extended forms. However, the extent of helicity was comparatively lower in Brevinin 1-Ya, irrespective of its starting structure in the simulations, and like other factors such as cationicity and hydrophobicity, could be related to the biological activity profiles of these peptides.

Palavras-chave : Brevinin; cationicity; anti-microbial peptides; MD; AMBER.

        · texto em Inglês     · Inglês ( pdf )

 

Creative Commons License Todo o conteúdo deste periódico, exceto onde está identificado, está licenciado sob uma Licença Creative Commons