Cargando…
Identification of GXXXXG motif in Chrysophsin-1 and its implication in the design of analogs with cell-selective antimicrobial and anti-endotoxin activities
Marine fish antimicrobial peptide, chrysophsin-1 possesses versatile biological activities but its non-selective nature restricts its therapeutic possibilities. Often small alterations in structural motifs result in significant changes in the properties of concerned proteins/peptides. We have identi...
Autores principales: | Tripathi, Amit Kumar, Kumari, Tripti, Harioudh, Munesh Kumar, Yadav, Pranjal Kumar, Kathuria, Manoj, Shukla, P. K., Mitra, Kalyan, Ghosh, Jimut Kanti |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5469811/ https://www.ncbi.nlm.nih.gov/pubmed/28611397 http://dx.doi.org/10.1038/s41598-017-03576-1 |
Ejemplares similares
-
Piscidin-1-analogs with double L- and D-lysine residues exhibited different conformations in lipopolysaccharide but comparable anti-endotoxin activities
por: Kumar, Amit, et al.
Publicado: (2017) -
Cell-Selective Pore Forming Antimicrobial Peptides
of the Prodomain of Human Furin: A Conserved Aromatic/Cationic Sequence
Mapping, Membrane Disruption, and Atomic-Resolution Structure and
Dynamics
por: Sinha, Sheetal, et al.
Publicado: (2018) -
An Unprecedented alteration in mode of action of IsCT resulting its translocation into bacterial cytoplasm and inhibition of macromolecular syntheses
por: Tripathi, Jitendra K., et al.
Publicado: (2015) -
Dynamics of Physical Interaction between HIV-1 Nef and ASK1: Identifying the Interacting Motif(S)
por: Kumar, Balawant, et al.
Publicado: (2013) -
Modern basal insulin analogs: An incomplete story
por: Singh, Awadhesh Kumar, et al.
Publicado: (2014)