Self-assembling antimicrobial peptides (SAAMPs) are promising candidates for antibiotic substitutes. The self-assembled structure provides proteolytic stability to the individual antimicrobial peptides. Since those need to target the bacterial membrane as unimers, the molecular exchange kinetics of the SAAMPs are of fundamental interest. In the proposed experiment we would like to investigate the exchange mechanism(s) of previously reported SAAMP-polymer conjugates. This will be achieved in a kinetic zero-average contras tscheme using time-resolved small-angle neutron scattering. By varying pH (assembly stability), temperature (exchange time) and sample concentration (collision-induced mechanisms), we will systematically study the molecular exchange pathways of SAAMPs, enabling the future tailoring in drug applications.