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Abstract:
Dermcidin (DCD) is an antimicrobial peptide, which is constitutively expressed in eccrine sweat glands. By post-secretory proteolytic processing in sweat the dermcidin protein gives rise to anionic and cationic DCD-peptides with a broad spectrum of antimicrobial activity. We could show that dermcidin-derived peptides inhibit significantly bacterial macromolecular synthesis (RNA, DNA, pro- tein) within the first minutes without binding to microbial DNA or RNA. Recent structural analysis indicated that the anionic 48mer peptide DCD-1L forms ion-dependent oligomeric structures which are able to interact with the bacterial cell envelope and perturb the bacterial membrane structure. Fur- ther investigations by CD-spectroscopy and conductance measurements with artificial phospholipid membranes suggest thatDCD-1L is able to form small pores in the bacterial membrane which leads to ion efflux and bacterial death. These data show for the first time how an antimicrobial peptide present in human eccrine sweat is able to kill efficiently several types of microorganisms.
