SciELO - Scientific Electronic Library Online

 
vol.65Alternative dissolution methods for analysis of niobium containing samplesSynthesis, characterization and antimicrobial studies of some novel 1,3,4-thiadiazolium-2-thiolate derivatives índice de autoresíndice de materiabúsqueda de artículos
Home Pagelista alfabética de revistas  

Servicios Personalizados

Articulo

Indicadores

Links relacionados

  • En proceso de indezaciónCitado por Google
  • En proceso de indezaciónSimilares en Google

Compartir


South African Journal of Chemistry

versión On-line ISSN 1996-840X
versión impresa ISSN 0379-4350

Resumen

SINGH, Parvesh  y  BISETTY, Krishna. A molecular dynamics study of lunasin. S.Afr.j.chem. (Online) [online]. 2012, vol.65, pp.115-124. ISSN 1996-840X.

Lunasin, a 43 amino acid peptide, suppresses chemically induced transformations in mammalian cells and skin carcinogenesis in mice. This peptide has also been reported to exhibit very good bioavailability after its oral administration. However, despite its biological and medicinal significance, the exact three-dimensional (3D) structure of lunasinis thus far not yet fully characterized. Thus this work is aimed at exploring the conformational profile of lunasin,using classical molecular dynamics (MD) simulations at the time scale of 300 ns. The results obtained from the MD trajectory reveal that lunasin has a strong propensity to exhibit three characteristic a helical bundles in its structure supported by residues His5-Cys10, Cys22-Ile30 and Asp35-Asp41. The reported cell adhesion motif (Arg-Gly-Asp) of lunasin responsible for its binding to cell chromatin, on other hand, did not exhibit any characteristic secondary feature. The structural information obtained from the current study could be useful to better understand the bioactive conformation of lunasin.

Palabras clave : Lunasin; molecular dynamics; amber; CLASICO; α-helix; β-turn; PTRAJ; RGD; RMSD.

        · texto en Inglés     · Inglés ( pdf )

 

Creative Commons License Todo el contenido de esta revista, excepto dónde está identificado, está bajo una Licencia Creative Commons