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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Solid phase peptide synthesis of human endothelin precursor peptides using two-step hard acid deprotection/cleavage methods.

Syntheses are described for the putative human and porcine biosynthetic precursors (hET-38 and pET-39) of endothelin, with the sequence previously deduced from human- and porcine-cDNA coding for preproendothelin. The Boc based solid phase synthetic method was applied, followed by weak hard acid, trimethylsilyl bromide, cleavage. The peptide removal from the resin was optimally accomplished with hydrogen fluoride. Disulfide bridges were formed by air-oxidation, and the linkage modes determined by enzymic (Endoproteinase Asp-N) digestion and HPLC. Five additional C-terminally elongated endothelin homologs were also synthesized. For alternative synthesis of pET-39, the use of trimethylsilyl trifluoromethanesulfonate for the removal of peptide from the resin generated a major side product, which was characterized. hET-38 was found to be less effective in vitro, when compared to endothelin. The vasoconstrictor activity in vitro of other related peptides was comparable to that of hET-38.[1]

References

  1. Solid phase peptide synthesis of human endothelin precursor peptides using two-step hard acid deprotection/cleavage methods. Nomizu, M., Inagaki, Y., Iwamatsu, A., Kashiwabara, T., Ohta, H., Morita, A., Nishikori, K., Otaka, A., Fujii, N., Roller, P.P. Int. J. Pept. Protein Res. (1991) [Pubmed]
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