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. 2016 Sep 1;6:32499. doi: 10.1038/srep32499

Figure 1. α- and θ-Defensins facilitate unfolding of viral proteins in DSF experiments.

Figure 1

Thermal denaturation profiles of HIV-1 proteins Gag-Δp6 (10 μM), CA (20 μM), RTp51 (10 μM), and IN (5 μM), as well as PFV IN (7 μM) and TEV protease (5 μM) were shifted toward lower temperatures in the presence of 3-fold molar excess of HNP-1 or 5-fold molar excess of RC-101 over the viral proteins. HD-5 caused destabilization of HIV-1 proteins Gag-Δp6 and CA and PFV IN. β-Defensin hBD-2 had no effect on any of the tested proteins. Human structural protein plastin-3 (PLS3) and serum IgG were not significantly affected by the defensins. See also Table 1.