l-Proline induced self-assembly of indolicidin derived palindromic tripeptide

We describe the synthesis, crystal structure, and various microscopic studies of the palindromic tripeptide WPW derived from antimicrobial peptide indolicidin. The present study reveals that tripeptide 1 and 2 undergo self-assembly to form vesicular structures after prolonged incubation, thus giving an interesting insight into the contribution of l-proline and flanking tryptophan residues in the self-assembly process. These vesicles were also amenable to simple focused ion beam (FIB)-aided bisection and thus possible to mill these vesicles to create different shapes. The circular dichroism (CD) analysis indicates that incubation promotes and stabilizes the more favorable secondary structures for 1 and 2. Preliminary result shows that tripeptide 1 exhibits appreciable interaction with Tb3+ as determined by quenching in tryptophan fluorescence.

The crystal structure and microscopic studies of the palindromic tripeptide WPW give interesting insight into contribution of l-proline and flanking tryptophan residues in the self-assembly process.Figure optionsDownload as PowerPoint slide