Bond-Specific Chemical Cleavages of Peptides and Proteins with Perfluoric Acid Vapors: Novel Peptide Bond Cleavages of Glycyl-Threonine, the Amino Side of Serine Residues and the Carboxyl Side of Aspartic Acid Residues

• Published in: Journal of biochemistry (Tokyo) 1997-01, Vol.121 (1), p.68-76
• Main Authors: Kawakami, Takao, Kamo, Masaharu, Takamoto, Keiji, Miyazaki, Kenji, Chow, Lu-Ping, Ueno, Yoshio, Tsugita, Akira
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Asp-C cleavage; Asp-Pro cleavage; Aspartic Acid - chemistry; cleavage; Fluorocarbons - chemistry; Gly-Thr cleavage; Glycine - chemistry; Molecular Sequence Data; Peptides - chemistry; perfluoric acid; Proline - chemistry; Proteins - chemistry; Ser-N; Serine - chemistry; Threonine - chemistry
• ISSN: 0021-924X
• DOI: 10.1093/oxfordjournals.jbchem.a021572

Peptide bond cleavages by vapors composed of various from aqueous solutions of perfluoric acid were studied using synthetic peptides and proteins, and specific conditions were established for peptide bond cleavages including a novel cleavage of the glycyl-threonine bond. The peptide bonds on the aminosides of serine residues were cleaved by exposure to a vapor of 75%aqueous heptafluorobutyric acid at 30 or 50°C for 24 h. Glycyl-threonine peptide bonds were cleaved with vapors of various concentrations (5, 75, and 90%) of heptafluorobutyric acid at 30–40°C for 24 h. The peptide bonds on the carboxylsides of aspartic acid residues were cleaved by exposure to a vapor of 0.2% heptafluorobutyric acid at 90°C for 4 to 24 h. The same vapor cleaved aspartyl-proline bonds under milder conditions such as at 60°C for 16 h, under which the other aspartyl bonds were uncleaved. These specific chemical cleavages were applied to several proteins including newly characterized proteins.