ArticleBiophysical journal2004
Electrospray ionization-mass spectrometry and tandem mass spectrometry reveal self-association and metal-ion binding of hydrophobic peptides: a study of the gramicidin dimer.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 32 citations in OpenAlex.
- Investigation of the potential ofFrontiers in microbiology · 2023Article
- Cu and Zn Interactions with Peptides Revealed by High-Resolution Mass Spectrometry.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Noncovalently Associated Peptides Observed during Liquid Chromatography-Mass Spectrometry and Their Effect on Cross-Link Analyses.Analytical chemistry · 2019Article
- Multiple solution structures of the disordered peptide indolicidin from IMS-MS analysis.International journal of mass spectrometry · 2018Article
- A Database of Transition-Metal-Coordinated Peptide Cross-Sections: Selective Interaction with Specific Amino Acid Residues.Journal of the American Society for Mass Spectrometry · 2017Article
- Article
- A database of alkaline-earth-coordinated peptide cross sections: insight into general aspects of structure.Journal of the American Society for Mass Spectrometry · 2013Article
- Analysis of amphiphilic lipids and hydrophobic proteins using nonresonant femtosecond laser vaporization with electrospray post-ionization.Journal of the American Society for Mass Spectrometry · 2011Article
- The gramicidin dimer shows both EX1 and EX2 mechanisms of H/D exchange.Journal of the American Society for Mass Spectrometry · 2009Article
- Determination of affinity constants and response factors of the noncovalent dimer of gramicidin by electrospray ionization mass spectrometry and mathematical modeling.Journal of the American Society for Mass Spectrometry · 2005Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Gramicidin is a membrane pentadecapeptide that acts as a channel, allowing the passage of monovalent metal ions and assisting in bacterial cell death. The active form is a noncovalently bound dimer. One means to study the self-assembly of this peptide has been to compare the state of the peptide in various solvents ranging from hydrophilic (e.g., trifluoroethanol) to hydrophobic (e.g., n-propanol). In this article, we report the use of electrospray mass spectrometry to study the self-association of gramicidin in various organic and mixed solvents that are introduced directly into the mass spectrometer. The dimer (both homo and hetero) can survive the introduction into the gas phase, and the amount in the gas phase increases with the decreasing dielectric constant of the solvent, reflecting solution-phase behavior. Tandem mass spectrometry data reveal that the stability of dimer in the gas phase decreases with increasing metal ion size, strongly suggesting that the metal ion binds inside the dimer between the monomers.
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Registered trials
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