ArticleEuropean biophysics journal : EBJ2010
Conformational studies of peptides representing a segment of TM7 from H+-VO-ATPase in SDS micelles.
Article in European biophysics journal : EBJ, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 8 citations in OpenAlex.
- Optimized Zebrafish AP2M1A-Derived Decapeptide AP10RW with Robust Stability Suppresses Multidrug-Resistant Bacteria.Biomolecules · 2026Article
- Peptide-Based Efflux Pump Inhibitors of the Small Multidrug Resistance Protein from Pseudomonas aeruginosa.Antimicrobial agents and chemotherapy · 2019Article
- Hydrophobic blocks facilitate lipid compatibility and translocon recognition of transmembrane protein sequences.Biochemistry · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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Abstract
The conformation of a transmembrane peptide, sMTM7, encompassing the cytoplasmic hemi-channel domain of the seventh transmembrane section of subunit a from V-ATPase from Saccharomyces cerevisiae solubilized in SDS solutions was studied by circular dichroism (CD) spectroscopy and fluorescence spectroscopy of the single tryptophan residue of this peptide. The results show that the peptide adopts an alpha-helical conformation or aggregated beta-sheet depending on the peptide-to-SDS ratio used. The results are compared with published data about a longer version of the peptide (i.e., MTM7). It is concluded that the bulky, positively charged arginine residue located in the center of both peptides has a destabilizing effect on the helical conformation of the SDS-solubilized peptides, leading to beta-sheet formation and subsequent aggregation.
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