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Fig. 5 | Journal of Nanobiotechnology

Fig. 5

From: Enhanced stability of a chimeric hepatitis B core antigen virus-like-particle (HBcAg-VLP) by a C-terminal linker-hexahistidine-peptide

Fig. 5

Effects of physical and chemical stress on the stability of chimeric VLPs with different polyhistidine-peptide lengths and on an alternative chimeric VLP. a Chimeric VLPs containing 0; 3; 6; 12 histidine residues (ΔHis, 3His, 6His, 12His) at the C-terminus were chemically (urea) or physically stressed (temperature). Effects on the capsid stability were analyzed by NAGE and dot blot (for details see Fig. 3). b Chimeric VLPs (6His2nd/ΔHis2nd) with a different epitope sequence and MIR-insertion site were chemically and physically stressed as described before, only stress-tests resulting in significant differences of the VLP stability are shown (urea and pH). All assays were performed in triplicates

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