Abstract
role in various functions, e.g. locomotor activity, nociception, arousal and thermoregulation (Griffiths, 1985). By using h.p.1.c. to determine the relative stabilities of the TRH analogues to degradation by a proline endopeptidase and a pyroglutamyl aminopeptidase (in the two subcellular fractions), the following descending order of stability was found: RX77368. CG3509, RX74355. MK771, TRH, [3-methyl-His]TRH, CG3703. It is suggested that both binding-affinity for TRH receptors and stability to degradation may contribute to the central actions of the analogue series studied; methylation of the proline residue (in RX74355 and RX77368) reduced metabolism without seriously influencing receptor binding. Conformational analysis of these analogues has shown a preferred conformer for central TRH actions with the histidyl and prolyl residues in close proximity (Ward et al., 1985), and it may be possible to combine theoretical structural considerations with information on receptor binding and stability to design novel analogues of TRH.
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