ArticleThe Biochemical journal1994
Mechanism of interaction between actin and membrane lipids: a pressure-tuning infrared spectroscopy study.
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 25 citations in OpenAlex.
- Shedding light on biochemical changes in single neuron-like pheochromocytoma cells following exposure to synchrotron sourced terahertz radiation using synchrotron source Fourier transform infrared microspectroscopy.Journal of synchrotron radiation · 2025Article
- Exploring the stability limits of actin and its suprastructures.Biophysical journal · 2014Article
- Induced secondary structure and polymorphism in an intrinsically disordered structural linker of the CNS: solid-state NMR and FTIR spectroscopy of myelin basic protein bound to actin.Biophysical journal · 2009Article
- Flavonoids affect actin functions in cytoplasm and nucleus.Biophysical journal · 2007Article
- Fluorescence generalized polarization of cell membranes: a two-photon scanning microscopy approach.Biophysical journal · 1996Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
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Abstract
Using pressure-tuning Fourier transform infrared spectroscopy to study an in vitro system consisting of actin and distearoyl-phosphatidylcholine (DSPC) liposomes, we have determined the mechanism of interaction between actin and membrane lipids. This interaction results in a significant conformational change in actin molecules. Analysis of the amide I band of actin shows an increase in the beta-sheets to alpha-helix ratio, in random turns, and in interactions between actin monomers. In the absence of lipids, the actin molecules are denatured by pressures of 8 x 10(8) Pa and more, which give rise to a random organization of the peptide chain. However, in the presence of DSPC liposomes, pressure greater than 2 x 10(8) Pa induces a change in actin conformation, which is dominated by strongly interacting beta-sheets. As the spectra of the lipid molecules are not changed by the presence of actin, the organization of the lipid molecules in the bilayer is not affected by the protein. It is concluded from these results that this interaction of actin with membrane lipids involves very few lipid molecules. These lipid molecules may interact with actin at a few specific sites on the protein.
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