Difference between revisions of "Part:BBa K3351003"
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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. | 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=== | ||
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| + | width: 60%;height: 60%;" src="https://static.igem.org/mediawiki/parts/d/d3/T--NWU-CHINA-A--od-1.png"><div>Figure.1 growth curve</div></html> | ||
===Reference=== | ===Reference=== | ||
Latest revision as of 10:38, 26 October 2020
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
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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]