NDLI: An Electrospray Ionization Mass Spectrometry Study on the “In Vacuo” Hetero-Oligomers Formed by the Antimicrobial Peptides, Surfactin and Gramicidin S

Content Provider	Springer Nature Link
Author	Rautenbach, Marina Vlok, N. Maré Eyéghé Bickong, Hans A. van der Merwe, Marthinus J. Stander, Marietjie A.
Copyright Year	2017
Abstract	It was previously observed that the lipopeptide surfactants in surfactin (Srf) have an antagonistic action towards the highly potent antimicrobial cyclodecapeptide, gramicidin S (GS). This study reports on some of the molecular aspects of the antagonism as investigated through complementary electrospray ionization mass spectrometry techniques. We were able to detect stable 1:1 and 2:1 hetero-oligomers in a mixture of surfactin and gramicidin S. The noncovalent interaction between GS and Srf, with the proposed equilibrium: GS~Srf↔GS+Srf correlated to apparent K $_{d}$ values of 6–9 μM in gas-phase and 1 μM in aqueous solution. The apparent K $_{d}$ values decreased with a longer incubation time and indicated a slow oligomerization equilibrium. Furthermore, the low μM K $_{d}$ $^{app}$ values of GS~Srf↔GS+Srf fell within the biological concentration range and related to the 2- to 3-fold increase in [GS] needed for bacterial growth inhibition in the presence of Srf. Competition studies indicated that neither Na$^{+}$ nor Ca$^{2+}$ had a major effect on the stability of preformed heterodimers and that GS in fact out-competed Ca$^{2+}$ and Na$^{+}$ from Srf. Traveling wave ion mobility mass spectrometry revealed near symmetrical peaks of the heterodimers correlating to a compact dimer conformation that depend on specific interactions. Collision-induced dissociation studies indicated that the peptide interaction is most probably between one Orn residue in GS and the Asp residue, but not the Glu residue in Srf. We propose that flanking hydrophobic residues in both peptides stabilize the antagonistic and inactive peptide hetero-oligomers and shield the specific polar interactions in an aqueous environment. Graphical Abstract ᅟ
Starting Page	1623
Ending Page	1637
Page Count	15
File Format	PDF
ISSN	10440305
Journal	Journal of The American Society for Mass Spectrometry
Volume Number	28
Issue Number	8
e-ISSN	18791123
Language	English
Publisher	Springer US
Publisher Date	2017-05-30
Publisher Institution	The American Society for Mass Spectrometry
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Surfactin Gramicidin S Lipopeptide Antimicrobial peptide Antagonism Molecular interaction Electrospray ionization mass spectrometry Analytical Chemistry Biotechnology Organic Chemistry Proteomics Bioinformatics
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Structural Biology

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