Substituting azobenzene for proline in melittin to create photomelittin: A light-controlled membrane active peptide

In this article we present the synthesis and characterization of a new form of the membrane active peptide melittin: photomelittin. This peptide was created by substituting the proline residue in melittin for a synthetic azobenzene amino acid derivative. This azobenzene altered the membrane activity of the peptide while retaining much of the secondary structure. Furthermore, the peptide demonstrates added light-dependent activity in leakage assays. There is a 1.5-fold increase in activity when exposed to UV light as opposed to visible light. The peptides further exhibit light-dependent hemolytic activity against human red blood cells. This will enable future studies optimizing photomelittin and other azobenzene-containing membrane active peptides for uses in medicine, drug delivery, and other biotechnological applications.

Automated summary

Photomelittin, a newly synthesized membrane active peptide, demonstrates light-dependent activity by substituting a specific amino acid derivative, showing promising applications in medicine, drug delivery, and biotechnological fields.