Application of molecular recognition theory in thyrotropin and its receptor system

AIM: The selective recognition of the sense peptides which are located in special regions of thyrotropin receptor (TSHR) by their corresponding antisense peptides has been investigated. Three pairs of sense and antisense peptides were named TR1 (aa37-45) and RT1 (aa45-37), TR2 (aa353-366) and RT2 (aa366-353), TR3 (aa648-655) and RT3 (aa655-648). METHODS: To prepare three affinity chromatography columns, antisense peptides were immobilized, called RT1-sepharose 4B, RT2-sepharose 4B and RT3-sepharose 4B, respectively and investigate the retardative behavior for each of native peptide TR1, TR2 or TR3 on above columns with stepwise elution. RESULTS: Each of the three immobilized antisense peptides recognized and retarded its corresponding sense peptide-TR1, TR2 or TR3 instead of those non-complementary peptides. Immobilized RT1 recognized free TSHR protein molecule as well. In additional, bovine thyrotropin was recognized by immobilized TR1. CONCLUSION: The results indicate that molecular recognition theory exsits in thyrotropin receptor system. It may be useful to isolate biological molecules and to locate epitopes of TSH on TSHR molecule. Otherwise, antisense peptide may be used for treatment of experimental autoimmunolized thyroid disease (AITD) in the rat.