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Orthosteric Binding of ρ-Da1a, a Natural Peptide of Snake Venom Interacting Selectively with the α_1A-Adrenoceptor

Figure 3

Influence of various ligands on ³H-prazosin and ¹²⁵I-HEAT dissociation.

Panel A: Dissociation of ³H-prazosin (2 nM) binding to α_1A-AR (1 µg) in the presence of prazosin (10 µM, black), prazosin plus ρ-Da1a (2.5 µM, blue), prazosin plus adrenaline (2 mM, red) and prazosin plus EPA (150 µM, green). Panel B : dissociation of ¹²⁵I-HEAT (0.4 nM) binding to α_1A-AR (0.2 µg) in the presence of HEAT (5 µM, black), HEAT plus ρ-Da1a (2.5 µM, blue), HEAT plus prazosin (10 µM, red) and HEAT plus EPA (150 µM, green). n = 2.

doi: https://doi.org/10.1371/journal.pone.0068841.g003