title: Design of a novel thymopoietin analogue based on conformational analyses.
abstract: A novel cyclic peptide c(Arg-Pro-Asp-D-Val-Tyr) related to thymopentin--the immunostimulant pentapeptide contained in thymic hormones--was designed on the basis of theoretical computer modeling. We applied molecular dynamics/energy minimization techniques and restrained molecular dynamics to determine the preferred conformation of this peptide. The linear precursor of the peptide is biologically active and probably exists in a highly motile dynamical equilibrium of different conformations. Our calculations show that the cyclic peptide consists of a single conformational family containing a beta turn at position Pro 2. Experimental support for this conclusion was derived from 2-D NOE data in aqueous solution for the closely related analogue c(Arg-Lys-Glu-D-Val-Tyr). Synthesis and biological testing of the cyclic peptide is therefore indicated.
authors.affiliation: Boris Kidric Institute of Chemistry, Ljubljana, Yugoslavia.
authors.forename: T
authors.initials: T
authors.lastname: Solmajer
mesh_terms: D000595:Amino Acid Sequence; D015195:Drug Design; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000138:chemical synthesis* / Q000737:chemistry; D011487:Protein Conformation; D016305:Thymopentin / Q000031:analogs & derivatives*; D013946:Thymopoietins / Q000138:chemical synthesis* / Q000737:chemistry
chemical_list: D010456:Peptides, Cyclic; D013946:Thymopoietins; C067938:cyclo(arginyl-prolyl-aspartyl-valyl-tyrosyl); D016305:Thymopentin