The synthesis of a small library of prospective growth hormone secretagogues

Employing tools of combinatorial chemistry, an original methodological approach has been developed and applied for the design and synthesis of a small library of peptide-like compounds, prospective growth hormone (GH) secretagogues. For this purpose seven building blocks of tBoc- and Fmoc-protected amino acids was used. In this way, a small, tripeptoid library on polyethylene glycolmonomethyl ether 5000 (PEG 5000) as a soluble support was obtained. The library was screened by a new, simple system, based on polyclonal rabbit antiserum raised against "GH secretagogue pharmacophore" of a known growth hormone secretagogue GHRP-6 (Hexarelin?) and the most promising GH secretagogue candidate was selected.

Purification and Characterization of Peach Mosaic Virus

Virus particles were observed by transmission electron microscopy in preparations extracted from symptomatic leaves of Chenopodium amaranticolor that had been mechanically inoculated with peach mosaic virus. The particles were long, flexuous, filamentous rods with an average length of 888 nm. Purified preparations had an A 260/280 nm ratio of 1.25. RNA extracted from purified virus was approximately 8.1 kilobases, and a capsid protein of approximately 27 kDa was found. Polyclonal rabbit antiserum, produced against purified virus, reacted with samples from peach mosaic and cherry mottle leaf-infected plants when used in Western blot analysis.