Abstract：
: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.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Bomar MG,Samuelsson SJ,Kibler P,Kodukula K,Galande AKdoi
10.1021/bm201836fsubject
Has Abstractpub_date
2012-03-12 00:00:00pages
579-83issue
3eissn
1525-7797issn
1526-4602journal_volume
13pub_type
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