Abstract
Many analogs of luteinizing hormone-releasing hormone (LH-RH) have been recently synthesized in order to investigate the significance of the various constituent amino acids in hormonal activity [ 1 ] . Assessments of the capacity of analogs to stimulate release of LH and FSH have revealed that arginine in position 8 on the peptide chain is critical for eliciting full activity [2-51. It was suggested that the basic guanidine side-chain of arginine participates in the binding of LH-RH to its specific pituitary receptor site via an ionic interaction [5] and probably by a hydrogen-bond formation mechanism, as well [3]. It was also postulated, based on fluorescence studies, that the importance of arginine is due to its location in the tertiary structure of the LH-RH molecule itself, that is, in the assembly of the amino acids His’, Tyr’, and Arg8 which exist as a close-knit unit, probably playing an active role in the hormonal action of the peptide [6,7]. The structural function of Arg* was also suggested by binding studies of LH-RH and several of its analogs to plasma membranes of the anterior pituitary [8] . To gain further understanding of the function of
Published Version (Free)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have