ArticleBiophysical journal2000
Solvent effects on the conformation of the transmembrane peptide gramicidin A: insights from electrospray ionization mass spectrometry.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Identification of novel Gramicidin S analogs from Aneurinibacillus aneurinilyticus isolated from corn steep liquor with potential antifungal activity.Microbial cell factories · 2025Article
- Effects of Calcium Ions on the Antimicrobial Activity of Gramicidin A.Biomolecules · 2022Article
- The Effect of Calcium and Halide Ions on the Gramicidin A Molecular State and Antimicrobial Activity.International journal of molecular sciences · 2020Article
- Design, synthesis, and biological evaluation of stable βEuropean journal of medicinal chemistry · 2018Article
- A conformational investigation of propeptide binding to the integral membrane protein γ-glutamyl carboxylase using nanodisc hydrogen exchange mass spectrometry.Biochemistry · 2014Article
- Cholesterol lowering drug may influence cellular immune response by altering MHC II function.Journal of lipid research · 2013Article
- Mass spectrometry--from peripheral proteins to membrane motors.Journal of molecular biology · 2012Review
- The membrane interface dictates different anchor roles for "inner pair" and "outer pair" tryptophan indole rings in gramicidin A channels.Biochemistry · 2011Article
- Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry.Analytical chemistry · 2010Article
- The preference of tryptophan for membrane interfaces: insights from N-methylation of tryptophans in gramicidin channels.The Journal of biological chemistry · 2008Article
- Electrospray ionization-mass spectrometry and tandem mass spectrometry reveal self-association and metal-ion binding of hydrophobic peptides: a study of the gramicidin dimer.Biophysical journal · 2004Article
- Hydrogen/deuterium exchange of hydrophobic peptides in model membranes by electrospray ionization mass spectrometry.Journal of the American Society for Mass Spectrometry · 2002Article
- Structure of melittin bound to phospholipid micelles studied using hydrogen-deuterium exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry.Journal of the American Society for Mass Spectrometry · 2001Article
- The methanol-induced conformational transitions of beta-lactoglobulin, cytochrome c, and ubiquitin at low pH: a study by electrospray ionization mass spectrometry.Journal of the American Society for Mass Spectrometry · 2001Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The binding of sodium ions to the transmembrane channel peptide gramicidin A has permitted the use of electrospray ionization mass spectrometry to study its conformation in different solvent environments. The mass spectra of the peptide in the various solvents suggest that different conformations of gramicidin A differ in their ability to bind metal ions. The data are consistent with monomeric behavior of gramicidin A in trifluoroethanol and dimethyl sulfoxide solutions, but reveal the presence of noncovalent intermolecular interactions in ethanol solution through the observation of heterodimers formed between the naturally occurring variants of the peptide. The addition of 50% v/v of water to the ethanolic solution causes changes in the circular dichroism spectrum of the peptide, suggestive of a shift in the equilibrium mixture of conformers present toward monomeric species, a result supported by its mass spectrum. The structure of gramicidin A in trifluoroethanol has also been investigated by hydrogen exchange measurements monitored by mass spectrometry. The observation of significant protection against exchange suggests that the monomeric peptide is highly structured in trifluoroethanol. The results indicate that mass spectrometry has the potential to probe the conformational behavior of neutral hydrophobic peptides in environments that mimic their functional states.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.