Part:BBa_K3351003

DCD1L, an antimicrobial peptide.

Summary

Human dermcidin (DCD) is an antimicrobial peptide secreted constitutively by sweat glands. The anionic derivative, DCD-1L, comprises of the N-terminal 47 residues of DCD and one additional leucine residue. DCD-1L is anionic, with a net charge of −5, and is amphipathic in nature. It has three helical regions and its cationic N-terminal part is proposed to interact with negatively charged phospholipid membranes of bacteria. On the bacterial membrane, studies suggest that the DCD-1L peptide first aligns flat with surface and then slowly forms oligomeric complexes, which are stabilized by Zn2+ and coordinated by the H38 residue. The oligomeric complex then breaks open, inserts into the membrane, and undergoes re-oligomerization to form the channel. The contents flow out though the channel and the bacterial die.

Characterization

Figure.1 growth curve

Reference

[1] Nguyen VS, Tan KW, Ramesh K, Chew FT, Mok YK. Structural basis for the bacterial membrane insertion of dermcidin peptide, DCD-1L. Sci Rep. 2017 Oct 24;7(1):13923. doi: 10.1038/s41598-017-13600-z. PMID: 29066724; PMCID: PMC5654962. Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE WITH RFC[1000]