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• W2024057497 abstract "We demonstrated a high level expression and purification of recombinant human immunodeficiency virus type 1 gp41 ectodomain (gp41e-FP) using glass bead approach with a final yield of 12±2mg/L bacterial culture. The proper folding of gp41e-FP encompassing the fusion peptide (FP) was ascertained by circular dichroism (CD) measurement and recognition by NC-1 antibody. The latter assay revealed stabilization of the gp41 coiled coil structure in the presence of liposome dispersion. The differential affinity of gp41e-FP and gp41e (devoid of FP) by NC-1 suggested an aggregated state for gp41e-FP and/or possible proximity of the fusion peptide domain to the coiled coil structure of gp41 ectodomain. Perfluorooctanoate (PFO)-PAGE electrophoresis experiment revealed the trimeric propensity of the recombinant gp41e-FP. In comparison to gp41e, the lipid mixing activity of gp41e-FP was two-fold higher suggesting a role of FP in promoting membrane fusion. The present approach to efficiently and quantitatively preparing the functional full-length recombinant gp41 ectodomain protein can be employed for structural and biomedical investigations and the extraction of other inclusion body-embedded recombinant proteins." @default.
• W2024057497 created "2016-06-24" @default.
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• W2024057497 date "2011-04-01" @default.
• W2024057497 modified "2023-09-26" @default.
• W2024057497 title "An efficient production and characterization of HIV-1 gp41 ectodomain with fusion peptide in Escherichia coli system" @default.
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• W2024057497 doi "https://doi.org/10.1016/j.jbiotec.2011.03.005" @default.
• W2024057497 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21419812" @default.
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