Deuterium Solid State NMR Studies of Intact Bacteria Treated With Antimicrobial Peptides

被引:9
作者
Booth, Valerie [1 ,2 ]
机构
[1] Mem Univ Newfoundland, Dept Biochem, St John, NF, Canada
[2] Mem Univ Newfoundland, Dept Phys & Phys Oceanog, St John, NF, Canada
来源
FRONTIERS IN MEDICAL TECHNOLOGY | 2021年 / 2卷
基金
加拿大自然科学与工程研究理事会;
关键词
HDP; AMP; intact bacteria; whole cell NMR; solid state NMR; magic angle spinning (MAS); lipid membrane; bilayer; MEMBRANE-ACTIVE PEPTIDES; IN-CELL NMR; MOLECULAR ARCHITECTURE; ANTICANCER ACTIVITIES; OLIGOMERIC STRUCTURE; ESCHERICHIA-COLI; LIPID-MEMBRANES; PORE FORMATION; PISCIDIN; MECHANISM;
D O I
10.3389/fmedt.2020.621572
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
Solid state NMR has been tremendously useful in characterizing the structure and dynamics of model membranes composed of simple lipid mixtures. Model lipid studies employing solid state NMR have included important work revealing how membrane bilayer structure and dynamics are affected by molecules such as antimicrobial peptides (AMPs). However, solid state NMR need not be applied only to model membranes, but can also be used with living, intact cells. NMR of whole cells holds promise for helping resolve some unsolved mysteries about how bacteria interact with AMPs. This mini-review will focus on recent studies using H-2 NMR to study how treatment with AMPs affect membranes in intact bacteria.
引用
收藏
页数:9
相关论文
共 108 条
[71]   2H Solid-State Nuclear Magnetic Resonance Investigation of Whole Escherichia coli Interacting with Antimicrobial Peptide MSI-78 [J].
Pius, James ;
Morrow, Michael R. ;
Booth, Valerie .
BIOCHEMISTRY, 2012, 51 (01) :118-125
[72]   Unambiguous Ex Situ and in Cell 2D 13C Solid-State NMR Characterization of Starch and Its Constituents [J].
Poulhazan, Alexandre ;
Arnold, Alexandre A. ;
Warschawski, Dror E. ;
Marcotte, Isabelle .
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2018, 19 (12)
[73]   In situ and real time investigation of the evolution of a Pseudomonas fluorescens nascent biofilm in the presence of an antimicrobial peptide [J].
Quiles, Fabienne ;
Saadi, Souhir ;
Francius, Gregory ;
Bacharouche, Jalal ;
Humbert, Francois .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2016, 1858 (01) :75-84
[74]   Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin [J].
Ramamoorthy, Ayyalusamy ;
Thennarasu, Sathiah ;
Lee, Dong-Kuk ;
Tan, Anmin ;
Maloy, Lee .
BIOPHYSICAL JOURNAL, 2006, 91 (01) :206-216
[75]   Focal Targeting of the Bacterial Envelope by Antimicrobial Peptides [J].
Rashid, Rafi ;
Veleba, Mark ;
Kline, Kimberly A. .
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY, 2016, 4
[76]   Peptidoglycan and Teichoic Acid Levels and Alterations in Staphylococcus aureus by Cell-Wall and Whole-Cell Nuclear Magnetic Resonance [J].
Romaniuk, Joseph A. H. ;
Cegelski, Lynette .
BIOCHEMISTRY, 2018, 57 (26) :3966-3975
[77]   How Many Antimicrobial Peptide Molecules Kill a Bacterium? The Case of PMAP-23 [J].
Roversi, Daniela ;
Luca, Vincenzo ;
Aureli, Simone ;
Park, Yoonkyung ;
Mangoni, Maria Luisa ;
Stella, Lorenzo .
ACS CHEMICAL BIOLOGY, 2014, 9 (09) :2003-2007
[78]   Role of Charge in Lipid Vesicle Binding and Vesicle Surface Saturation by Gaduscidin-1 and Gaduscidin-2 [J].
Sandhu, Gagandeep ;
Booth, Valerie ;
Morrow, Michael R. .
LANGMUIR, 2020, 36 (33) :9867-9877
[79]   Progression of NMR studies of membrane-active peptides from lipid bilayers to live cells [J].
Sani, M. -A. ;
Separovic, F. .
JOURNAL OF MAGNETIC RESONANCE, 2015, 253 :138-142
[80]   How Membrane-Active Peptides Get into Lipid Membranes [J].
Sani, Marc-Antoine ;
Separovic, Frances .
ACCOUNTS OF CHEMICAL RESEARCH, 2016, 49 (06) :1130-1138