The amino terminal regions of proBNP and proANP oligomerise through leucine zipper-like coiled-coil motifs

We provide the first report of unique leucine zipper-like coiled-coil seque nce motifs at the amino terminus (N-) of proBrain Natriuretic Peptide (proB NP) and proArtial Natriuretic Peptide (proANP). These motifs were highly co nserved across most of the known natriuretic peptide sequences from differe nt species. Consistent with computer based modelling predictions, size excl usion (SE) chromatography analysis confirmed human and ovine N-BNP, N-ANP a nd human proBNP in plasma extracts to elute as high molecular weight oligom ers. Synthetic model peptides corresponding to the proposed leucine zipper- like coiled-coil regions of proBNP, proANP and their related N-terminal pep tides were shown to be sufficient to induce oligomerisation when assessed o n size exclusion HPLC. To our knowledge, this is the first report of circul ating peptides that oligomerise through leucine zipper-like coiled-coil mot ifs, and adds a new dimension to the held of vasoactive peptide research. ( C) 1999 Academic Press.