Abstract
In order to fully characterize the activity spectrum and additional biochemical properties of native antimicrobial peptides corresponding to chromogranin A, we synthesized glycosylated, phosphorylated and double modified versions of the reportedly antibacterial 173-194 fragment. While no conformational change was detected, the modifications stabilized the peptide from proteolytic cleavage. All peptides remained inactive against a number of Gram-positive and Gram-negative bacterial strains in the experimental conditions use.