Pyridoxal Associated Peptide Constructs

Baltzer and co-workers have utilized a synthetic peptide scaffold to incorporate features of transaminase enzymes [ 13]. Using this approach, they have attempted to achieve the selective and tight binding of a pyridoxal phosphate coenzyme observed in transaminase enzymes. A synthetic helix-turn-helix peptide known to dimerize into a four-helix bundle was chosen as the platform for design [5]. 

Binding of pyridoxal phosphate to peptide PP-42 also appears to be selective for lysine 30. As was indicated by NMR spectroscopy and UV/vis experiments, only one of three potential lysine Schiff bases appeared to form. To determine the site or sites of attachment, the aldimine peptide intermediates were reduced, proteolytically cleaved, and the fragments analyzed by mass spectroscopy. This 

This designed construct, as such, may not influence subsequent steps of transamination due to loss of the strong association between the coenzyme and the synthetic peptide after amino acid binding. However, the selectivity of the peptide for pyridoxal phosphate reveals the potential power of peptide design and the importance of secondary binding interactions for defining the formation of specific binary complexes. 

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