On antisense peptides: the parathyroid hormone as an experimental example and a critical theoretical view.
We followed an approach which predicts that translation of two complementary RNA strands into protein generates pairs of "antisense" peptides which bind each other with specific and high affinity (Bost et al. Proc. Natl. Acad. Sci. (1985) 82, 1372). We used human parathormone as an experimental example, and we analysed by computer homologies between antisense peptide sequences and their published receptor sequences. We conclude that there is no experimental indication that parathormone binds to a synthetic peptide, the sequence of which was derived from the antisense RNA sequence. Based on homology scores and antigenicity indexes (Hopp) the analysis shows that the peptide ligand itself, or a random artificial peptide, are as good candidates as the antisense peptide in producing antibodies, presumably recognizing the receptor. We therefore question the general applicability of this approach.
D000595:Amino Acid Sequence; D008954:Models, Biological; D010281:Parathyroid Hormone / Q000235:genetics / Q000276:immunology; D010455:Peptides / Q000138:chemical synthesis / Q000276:immunology; D011485:Protein Binding; D011487:Protein Conformation; D012313:RNA; D016372:RNA, Antisense; D011956:Receptors, Cell Surface / Q000378:metabolism; D018016:Receptors, Parathyroid Hormone; D012689:Sequence Homology, Nucleic Acid
D010281:Parathyroid Hormone; D010455:Peptides; D016372:RNA, Antisense; D011956:Receptors, Cell Surface; D018016:Receptors, Parathyroid Hormone; D012313:RNA