Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41598-017-13600-z
Title: Structural basis for the bacterial membrane insertion of dermcidin peptide, DCD-1L
Authors: Van, Sang Nguyen 
Tan, Kang Wei 
Ramesh, Karthik 
Chew, Fook Tim 
Mok, Yu Keung 
Keywords: Science & Technology
Multidisciplinary Sciences
Science & Technology - Other Topics
ANTIMICROBIAL PEPTIDE
C-13/N-15-ENRICHED PROTEINS
NMR-SPECTROSCOPY
ECCRINE SWEAT
RESONANCES
ASSIGNMENT
BACKBONE
SKIN
MECHANISM
GLANDS
Issue Date: 24-Oct-2017
Publisher: NATURE PUBLISHING GROUP
Citation: 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
Abstract: © 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.
Source Title: SCIENTIFIC REPORTS
URI: https://scholarbank.nus.edu.sg/handle/10635/168520
ISSN: 2045-2322
DOI: 10.1038/s41598-017-13600-z
Appears in Collections:Staff Publications
Elements

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
DCD paper supplementary materials_19 Sep 2017.docSupporting information139.5 kBMicrosoft Word

OPEN

NoneView/Download
DCD1L paper final version.pdfPublished version1.97 MBAdobe PDF

OPEN

PublishedView/Download

SCOPUSTM   
Citations

4
checked on Nov 23, 2020

Page view(s)

63
checked on Nov 20, 2020

Download(s)

3
checked on Nov 20, 2020

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.