Please use this identifier to cite or link to this item:
|Structural basis for the bacterial membrane insertion of dermcidin peptide, DCD-1L
|Van, Sang Nguyen
Tan, Kang Wei
Chew, Fook Tim
Mok, Yu Keung
|Science & Technology
Science & Technology - Other Topics
|NATURE PUBLISHING GROUP
|Van, Sang Nguyen, Tan, Kang Wei, Ramesh, Karthik, Chew, Fook Tim, Mok, Yu Keung (2017-10-24). Structural basis for the bacterial membrane insertion of dermcidin peptide, DCD-1L. SCIENTIFIC REPORTS 7 (1). ScholarBank@NUS Repository. https://doi.org/10.1038/s41598-017-13600-z
|© 2017 The Author(s). 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. A previous NMR structure of DCD-1L in 50% TFE showed a partial helical conformation, and its crystal structure in the presence of Zn2+ outlined a hexameric linear α-helical bundle. Three different models to describe membrane insertion were proposed but no conclusion was drawn. In the current study, the NMR structure of DCD-1L in SDS micelles showed an "L-shaped" molecule with three fully formed α-helices connected by flexible turns. Formation of these helices in DCD-1L in the presence of POPG vesicles suggests that the acidic C-terminal region of DCD-1L can suppress the binding of DCD-1L to POPG vesicles at basic but not acidic pH. Mutation of charged residues on the N-terminal and C-terminal regions of DCD-1L cause differences in POPG binding, suggesting distinct functional roles for these two regions. Charged residues from these two regions are also found to differentially affect Zn2+ coordination and aggregation of DCD-1L in the absence or presence of SDS, as monitored by 1D NMR. Our data agrees with one of the three models proposed.
|Appears in Collections:
Show full item record
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.