Interactions of the peptide �-neoendorphin (�-NE) with DNA have been investigated in the presence of porphyrin using dynamic light scattering (DLS), fluorescence, UV visible, and infrared techniques. Infrared spectra with curve-fitting procedure revealed that �-NE adopts a mixture of turns and �-sheet structures in aqueous solution. The secondary structure was altered in the presence of DNA and porphyrin. UV visible spectra show changes in Soret bands with bathochromic shifts when DNA binds to the peptide-porphyrin complex, and hypsochromic shifts when porphyrin is added to the peptide-DNA complex. Fluorescence spectra, with respect to the tyrosine residue, indicate that tyrosine residue is buried in the native peptide, and the peptide-porphyrin complex is very sensitive to the presence of DNA. DLS experiments indicated that �-NE forms aggregates in solution. Peptide-porphyrin complex was found to be smaller than peptide-DNA complex, and higher concentrations of porphyrin were found to destabilize the peptide-DNA complex.

Interactions of the cationic peptide β-neoendorphin with DNA in the presence of porphyrin

245th National Meeting (2013)

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