Impact of macromolecular crowding on the mesomorphic behavior of lipid self-assemblies
| Autor: | Agustín Mangiarotti, Luis A. Bagatolli |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Polymers
Molecular Conformation Biophysics Supramolecular chemistry Serum Albumin Human Biochemistry Glycerides Polyethylene Glycols Polymorphism (biophysics) 2-Naphthylamine Protein secondary structure chemistry.chemical_classification Aqueous solution Chemistry Water Cell Biology Polymer Lipids Random coil Immunoglobulin G Phosphatidylcholines Gelatin Macromolecular crowding Laurates Macromolecule |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 1863:183728 |
| ISSN: | 0005-2736 |
| DOI: | 10.1016/j.bbamem.2021.183728 |
| Popis: | Using LAURDAN fluorescence we observed that water dynamics measured at the interface of DOPC bilayers can be differentially regulated by the presence of crowded suspensions of different proteins (HSA, IgG, Gelatin) and PEG, under conditions where the polymers are not in direct molecular contact with the lipid interface. Specifically, we found that the decrease in water dipolar relaxation at the membrane interface correlates with an increased fraction of randomly oriented (or random coil) configurations in the polymers, as Gelatin > PEG > IgG > HSA. By using the same experimental strategy, we also demonstrated that structural transitions from globular to extended conformations in proteins can induce transitions between lamellar and non-lamellar phases in mixtures of DOPC and monoolein. Independent experiments using Raman spectroscopy showed that aqueous suspensions of polymers exhibiting high proportions of randomly oriented conformations display increased fractions of tetracoordinated water, a configuration that is dominant in ice. This indicates a greater capacity of this type of structure for polarizing water and consequently reducing its chemical activity. This effect is in line with one of the tenets of the Association Induction Hypothesis, which predicts a long-range dynamic structuring of water molecules via their interactions with proteins (or other polymers) showing extended conformations. Overall, our results suggest a crucial role of water in promoting couplings between structural changes in macromolecules and supramolecular arrangements of lipids. This mechanism may be of relevance to cell structure/function when the crowded nature of the intracellular milieu is considered. |
| Databáze: | OpenAIRE |
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