ArticleBiophysical journal2011
Tryptophan-lipid interactions in membrane protein folding probed by ultraviolet resonance Raman and fluorescence spectroscopy.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 102 citations in OpenAlex.
- Physicochemical Characteristics of Amphipathic Peptides and Their Cytotoxic Effects on Cancer and Normal Cell Lines.International journal of molecular sciences · 2026Article
- Identification of intracellular target of antimicrobial peptide EWAMP-R in bacteria.Communications biology · 2026Article
- Deep UV Resonance Raman Spectroscopy: Applications to Membrane Proteins and Peptides.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Trp31 Residue of Trx-1 Is Essential for Maintaining Antioxidant Activity and Cellular Redox Defense Against Oxidative Stress.Antioxidants (Basel, Switzerland) · 2025Article
- Lighting the Path: Raman Spectroscopy's Journey Through the Microbial Maze.Molecules (Basel, Switzerland) · 2024Article
- The antimicrobial fibupeptide lugdunin forms water-filled channel structures in lipid membranes.Nature communications · 2024Article
- Tryptophanyl-tRNA synthetase-1 (WARS-1) depletion and high tryptophan concentration lead to genomic instability in Caenorhabditis elegans.Cell death discovery · 2024Article
- Novel autosomal dominant TMC1 variants linked to hearing loss: insight into protein-lipid interactions.BMC medical genomics · 2023Article
- Evidence that specific interactions play a role in the cholesterol sensitivity of G protein-coupled receptors.Biochimica et biophysica acta. Biomembranes · 2021Article
- New Tmc1 Deafness Mutations Impact Mechanotransduction in Auditory Hair Cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Investigating the lipid fingerprint of SLC6 neurotransmitter transporters: a comparison of dDAT, hDAT, hSERT, and GlyT2.BBA advances · 2021Article
- Article
- The Trp-rich Antimicrobial Amphiphiles With Intramolecular Aromatic Interactions for the Treatment of Bacterial Infection.Frontiers in microbiology · 2021Article
- The Uniqueness of Tryptophan in Biology: Properties, Metabolism, Interactions and Localization in Proteins.International journal of molecular sciences · 2020Review
- The structural basis for monoclonal antibody 5D2 binding to the tryptophan-rich loop of lipoprotein lipase.Journal of lipid research · 2020Article
- Folding of the β-Barrel Membrane Protein OmpA into Nanodiscs.Biophysical journal · 2020Article
- Binding of the Anti-FIV Peptide C8 to Differently Charged Membrane Models: From First Docking to Membrane Tubulation.Frontiers in chemistry · 2020Article
- Functional and Pharmacological Characterization of the Rare CFTR Mutation W361R.Frontiers in pharmacology · 2020Article
- How to evaluate the cellular uptake of CPPs with fluorescence techniques: Dissecting methodological pitfalls associated to tryptophan-rich peptides.Biochimica et biophysica acta. Biomembranes · 2019Article
- Preferential Equilibrium Partitioning of Positively Charged Tryptophan into Phosphatidylcholine Bilayer Membranes.The journal of physical chemistry. B · 2019Article
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4 authors at 1 institution in 1 country.
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Abstract
Aromatic amino acids of membrane proteins are enriched at the lipid-water interface. The role of tryptophan on the folding and stability of an integral membrane protein is investigated with ultraviolet resonance Raman and fluorescence spectroscopy. We investigate a model system, the β-barrel outer membrane protein A (OmpA), and focus on interfacial tryptophan residues oriented toward the lipid bilayer (trp-7, trp-170, or trp-15) or the interior of the β-barrel pore (trp-102). OmpA mutants with a single tryptophan residue at a nonnative position 170 (Trp-170) or a native position 7 (Trp-7) exhibit the greatest stability, with Gibbs free energies of unfolding in the absence of denaturant of 9.4 and 6.7 kcal/mol, respectively. These mutants are more stable than the tryptophan-free OmpA mutant, which exhibits a free energy of unfolding of 2.6 kcal/mol. Ultraviolet resonance Raman spectra of Trp-170 and Trp-7 reveal evolution of a hydrogen bond in a nonpolar environment during the folding reaction, evidenced by systematic shifts in hydrophobicity and hydrogen bond markers. These observations suggest that the hydrogen bond acceptor is the lipid acyl carbonyl group, and this interaction contributes significantly to membrane protein stabilization. Other spectral changes are observed for a tryptophan residue at position 15, and these modifications are attributed to development of a tryptophan-lipid cation-π interaction that is more stabilizing than an intraprotein hydrogen bond by ∼2 kcal/mol. As expected, there is no evidence for lipid-protein interactions for the tryptophan residue oriented toward the interior of the β-barrel pore. These results highlight the significance of lipid-protein interactions, and indicate that the bilayer provides more than a hydrophobic environment for membrane protein folding. Instead, a paradigm of lipid-assisted membrane protein folding and stabilization must be adopted.
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