Disease relevance of Asp-pro

• A series of truncated Herpes simplex virion peptides studied by fast atom bombardment mass spectrometry under high and low energy collision induced dissociation conditions showed preferential fragmentation of the aspartyl-proline amide bond, compared to other peptide bonds [1].
• Escherichia coli expression vectors encoding an acid-labile aspartyl-proline (Asp-Pro) dipeptide bridging two protein sequences were constructed and used to synthesize two different bovine growth hormone (bGH) fusion proteins [2].

High impact information on Asp-pro

• In addition, there were isolated 6 peptides, produced by anomalous cleavage at the carboxyl groups of tryptophan residues, and two by hydrolysis of an aspartyl-proline bond [3].
• However, under certain conditions, which are not fully understandable at present, dipeptidyl peptidase IV releases more slowly a second dipeptide, aspartyl-proline, from pro-colipase, and this results in a partial activation [4].

References