Assessing topology and surface orientation of an antimicrobial peptide magainin 2 using mechanically aligned bilayers and electron paramagnetic resonance spectroscopy.

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Tytuł:: Assessing topology and surface orientation of an antimicrobial peptide magainin 2 using mechanically aligned bilayers and electron paramagnetic resonance spectroscopy.
Autorzy:: Mayo DJ; Department of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, United States.
Sahu ID; Department of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, United States.
Lorigan GA; Department of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, United States. Electronic address: .
Źródło:: Chemistry and physics of lipids [Chem Phys Lipids] 2018 Jul; Vol. 213, pp. 124-130. Date of Electronic Publication: 2018 Apr 22.
Typ publikacji:: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
Język:: English
Imprint Name(s):: Publication: Limerick : Elsevier Science Ireland Ltd
Original Publication: Amsterdam.
MeSH Terms:: Lipid Bilayers/*chemistry
Magainins/*chemistry
Amino Acid Sequence ; Antimicrobial Cationic Peptides/chemistry ; Antimicrobial Cationic Peptides/metabolism ; Cyclic N-Oxides/chemistry ; Electron Spin Resonance Spectroscopy ; Lipid Bilayers/metabolism ; Magainins/chemical synthesis ; Magainins/metabolism ; Spin Labels
Contributed Indexing:: Keywords: Antimicrobial peptides; CW-EPR; Electron paramagnetic resonance; Glass plate alignment; Magainin 2; Mechanical alignment; Solid phase peptide synthesis; Topology
Substance Nomenclature:: 0 (Antimicrobial Cationic Peptides)
0 (Cyclic N-Oxides)
0 (Lipid Bilayers)
0 (Magainins)
0 (Spin Labels)
XDN8H1XM17 (2,2,6,6-tetramethylpiperidine-N-oxide-4-amino-4-carboxylic acid)
Entry Date(s):: Date Created: 20180425 Date Completed: 20190122 Latest Revision: 20190122
Update Code:: 20240105
DOI:: 10.1016/j.chemphyslip.2018.04.004
PMID:: 29689258
: Czasopismo naukowe

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Aligned CW-EPR membrane protein samples provide additional topology interactions that are absent from conventional randomly dispersed samples. These samples are aptly suited to studying antimicrobial peptides because of their dynamic peripheral topology. In this study, four consecutive substitutions of the model antimicrobial peptide magainin 2 were synthesized and labeled with the rigid TOAC spin label. The results revealed the helical tilts to be 66° ± 5°, 76° ± 5°, 70° ± 5°, and 72° ± 5° for the TOAC substitutions H7, S8, A9, and K10 respectively. These results are consistent with previously published literature. Using the EPR (electron paramagnetic resonance) mechanical alignment technique, these substitutions were used to critically assess the topology and surface orientation of the peptide with respect to the membrane. This methodology offers a rapid and simple approach to investigate the structural topology of antimicrobial peptides.
(Copyright © 2018 Elsevier B.V. All rights reserved.)

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