63155-83-9Relevant academic research and scientific papers
Effect of obligatory replacement and conformational restriction on psychotropic activity of thyroliberin analogs
Masurov,Korotenko,Gorbatyuk,Shapiro,Mazepa,Dyadenko,Andronati
, p. 1960 - 1964 (1998)
Easy lactamization of Gln(Asn)-Pro-NH2 with the formation of cyclic dipeptides with the diketopiperazine structure (mimetics of the conformational fragments of linear tripeptides with the X-Pro trans-bond) was observed in the synthesis of tripeptide Glp-Gln-Pro-NH2 modified by the replacement of histidinc with obligatory similar glutamine in thyroliberin (Glp-His-Pro-NH2, TRH) and in the synthesis of its structural analog [Asn2]TRH. Ion peaks corresponding to the Glp and Pro amino acid residues were revealed in the mass spectra of the peptides synthesized. The biological properties of the compounds obtained were determined indicating that the obligatory replacement resulted in an increased physiological specificity of [Gln2]TRH. The enhanced activity of conformationally restricted cyclic peptides compared to linear ones suggests that the biologically active conformation responsible for the antidepressant activity of linear TRH analogs is the conformation with X-Pro trans-bond.
Pyroglutamide derivatives
-
, (2008/06/13)
Pyroglutamide derivatives have been found to be useful as nootropic agents for administration to humans and animals.
L-pyroglutamyl-L-prolinamide
-
, (2008/06/13)
L-pyroglutamyl-L-prolinamide is useful for correcting metabolic or endocrinal disorders connected with senescence. It can be prepared by reacting L-pyroglutamic acid with L-prolinamide.
