ArticleThe journal of physical chemistry. B2017
Sequence-Dependent Interfacial Adsorption and Permeation of Dipeptides across Phospholipid Membranes.
Article in The journal of physical chemistry. B, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Detecting and quantifying liquid-liquid phase separation in living cells by model-free calibrated half-bleaching.Nature communications · 2022Article
- Lipid-A-dependent and cholesterol-dependent dynamics properties of liposomes from gram-negative bacteria in ESKAPE.Scientific reports · 2022Article
- Oil Phase Solubility Rather Than Diffusivity Determines the Release of Entrapped Amino Acids and Di-Peptides from Water-in-Oil-in-Water Emulsions.Molecules (Basel, Switzerland) · 2022Article
- Fast bilayer-micelle fusion mediated by hydrophobic dipeptides.Biophysical journal · 2021Article
- Partition of Positively and Negatively Charged Tryptophan Ions in Membranes with Inverted Phospholipid Heads: Simulations and Experiments.The journal of physical chemistry. B · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We investigate permeation of three blocked dipeptides with different side chain polarity across a phospholipid membrane and their behavior at the water-membrane interface by way of molecular dynamics simulations. Hydrophilic serine-serine dipeptide is found to desorb from the interface to aqueous phase, whereas hydrophobic phenylalanine-leucine and amphiphilic serine-leucine tend to accumulate at the interface with a free energy minimum of -3 kcal/mol. All three dipeptides exhibit free energy barriers to permeation across the membrane located at the center of the bilayer. The height of the barrier is strongly sequence dependent and increases with the dipeptide polarity. It is equal to 3.5, 6.4, and 10.0 kcal/mol for phenylalanine-leucine, serine-leucine, and serine-serine, respectively. The corresponding permeability coefficients are equal to 4.6 × 10
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Registered trials
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