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Guangshun Wang   Professor  Institute, Department or Faculty Head 
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Guangshun Wang published an article in April 2019.
Research Keywords & Expertise See all
0 A
0 Antiviral
0 Innate Immunity
0 NMR Spectroscopy
0 Structural
0 antimicrobial peptide
Top co-authors See all
Nongnuj Tanphaichitr

87 shared publications

Department of Obstetrics and GynecologyFaculty of Medicine, University of Ottawa, Ottawa, Canada

Mark A. Baker

65 shared publications

Priority Research Centre in Reproductive Science, School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW 2308, Australia

Yuxiang Dong

27 shared publications

College of Pharmacy and ‡Eppley Institute for Research in Cancer, University of Nebraska Medical Center, Omaha, Nebraska 68198, United States

Kessiri Kongmanas

12 shared publications

Department of BiochemistryMicrobiology Immunology, Faculty of Medicine, University of Ottawa, Ottawa, Canada

Biswajit Mishra

6 shared publications

Department of Pathology and Microbiology; College of Medicine; University of Nebraska Medical Center; 985900 Nebraska Medical Center Omaha NE 68198-5900 USA

61
Publications
43
Reads
0
Downloads
1059
Citations
Publication Record
Distribution of Articles published per year 
(2002 - 2018)
Total number of journals
published in
 
31
 
Publications See all
BOOK-CHAPTER 0 Reads 0 Citations Design of Antimicrobial Peptides: Progress Made with Human Cathelicidin LL-37 Guangshun Wang, Jayaram Lakshmaiah Narayana, Biswajit Mishra... Published: 13 April 2019
Methods in Molecular Biology, doi: 10.1007/978-981-13-3588-4_12
DOI See at publisher website
Article 0 Reads 3 Citations Antibacterial, antifungal, anticancer activities and structural bioinformatics analysis of six naturally occurring tempo... Biswajit Mishra, Xiuqing Wang, Tamara Lushnikova, Yingxia Zh... Published: 01 August 2018
Peptides, doi: 10.1016/j.peptides.2018.05.011
DOI See at publisher website
Article 5 Reads 2 Citations Amino Acid Composition Determines Peptide Activity Spectrum and Hot-Spot-Based Design of Merecidin Xiuqing Wang, Biswajit Mishra, Tamara Lushnikova, Jayaram La... Published: 26 March 2018
Advanced Biosystems, doi: 10.1002/adbi.201700259
DOI See at publisher website
BOOK-CHAPTER 0 Reads 0 Citations List of Contributors Shekhar Agnihotri, Abdellah Ajji, Steven Arcidiacono, Nury A... Published: 01 January 2018
Handbook of Antimicrobial Coatings, doi: 10.1016/b978-0-12-811982-2.01002-7
DOI See at publisher website
BOOK-CHAPTER 0 Reads 0 Citations Mechanism of Action of Tethered Antimicrobial Peptides Guangshun Wang, Biswajit Mishra Published: 01 January 2018
Handbook of Antimicrobial Coatings, doi: 10.1016/b978-0-12-811982-2.00024-x
DOI See at publisher website
Article 0 Reads 3 Citations The π Configuration of the WWW Motif of a Short Trp-rich Peptide Is Critical for Targeting Bacterial Membranes, Disrupti... D. Zarena, Biswajit Mishra, Tamara Lushnikova, Fangyu Wang, ... Published: 26 July 2017
Biochemistry, doi: 10.1021/acs.biochem.7b00456
DOI See at publisher website PubMed View at PubMed ABS Show/hide abstract
Tryptophan-rich peptides, being short and suitable for large-scale chemical synthesis, are attractive candidates for developing a new generation of antimicrobials to combat antibiotic-resistant bacteria (superbugs). Although there are numerous pictures for membrane-bound structure of a single tryptophan (W), how multiple Trp amino acids assemble themselves and interact with bacterial membranes are poorly understood. This communication presents the three-dimensional structure for an eight-residue Trp-rich peptide (WWWLRKIW-NH2 with 50% W) determined by the improved 2D NMR method, which includes the measurements of 13C and 15N chemical shifts at natural abundance. This peptide forms the shortest two-turn helix with a distinct amphipathic feature. A unique structural arrangement is identified for the Trp triplet, WWW, that forms a π configuration with W2 as the horizontal bar and W1/W3 forming the two legs. Arginine scan reveals that the WWW motif is essential for killing methicillin-resistant Staphylococcus aureus USA300 and disrupting preformed bacterial biofilms. This unique π configuration for the WWW motif is stabilized by aromatic-aromatic interactions as evidenced by ring current shifts as well as nuclear Overhauser effects. By maintaining the WWW motif, a change of I7 to R led to a potent antimicrobial and antibiofilm peptide with four-fold improvement in cell selectivity. Collectively, this study elucidated the structural basis of antibiofilm activity of the peptide, identified a better peptide candidate via structure-activity relationship studies, and laid the foundation for engineering future antibiotics based on the WWW motif.
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