Specific reduction of carboxyl groups in peptides and proteins by diborane

• Published in: Biochemical Journal
• Main Authors: Atassi, M. Z., Rosenthal, Arthur F.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Portland Press Ltd. 1969
• Subjects: Sperm whale
• Online Access: http://dx.doi.org/10.1042/bj1110593; https://portlandpress.com/biochemj/article-pdf/111/4/593/762860/bj1110593.pdf

1. The reaction of several peptides and proteins with diborane was studied under different conditions to determine those most suitable for the specific reduction of carboxyl groups. 2. In the reaction of model peptides and the cyclic peptides bacitracin and tyrocidin, reduction at 0° was entirely specific for the carboxyl groups without affecting the peptide bonds. Acid amide residues were not reduced. Some tripeptides showed anomalous results in that the C-terminal residue was quite resistant to reduction. 3. Specific reduction of carboxyl groups was achieved in each of the following proteins: human serum albumin, egg albumin, adult human haemoglobin, sperm-whale apomyoglobin, horse heart cytochrome c and egg-white lysozyme. The C-terminal amino acid was usually reduced. 4. Conditions for specific reduction of all available carboxyl groups are not easily found and may vary from one substance to another. Specific reduction of a limited number of available carboxyl groups may be generally accomplished by reactions at −10°. 5. It is suggested that this chemical modification, which has the advantage of permanence, may be useful in studying the role of carboxyl groups in the conformation of proteins and in the biological properties of peptides and proteins.