1 research outputs found
Hemopressin Forms Self-Assembled Fibrillar Nanostructures under Physiologically Relevant Conditions
The nonapeptide hemopressin,
which is derived from the α chain of hemoglobin, has been reported
to exhibit inverse agonist activity against the CB1 receptor. Administration
of this peptide in animal models led to decreased food intake and
elicited hypotensive and antinociceptive effects. On the basis of
hemopressin’s potential in therapeutic applications and the
lack of a structure–activity relationship study in literature,
we aimed to determine the conformational
features of hemopressin under physiological conditions. We conducted
transmission electron microscopy experiments of hemopressin, revealing
that it self-assembles into fibrils under aqueous conditions at pH
7.4. Circular dichroism and nuclear magnetic resonance experiments
indicate that the peptide adopts a mostly extended β-like structure,
which may contribute to its self-assembly and fibril formation