ArticleBiochemistry and biophysics reports2019
A LEA model peptide protects the function of a red fluorescent protein in the dry state.
Article in Biochemistry and biophysics reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance inInternational journal of molecular sciences · 2022Article
- Natural and Designed Proteins Inspired by Extremotolerant Organisms Can Form Condensates and Attenuate Apoptosis in Human Cells.ACS synthetic biology · 2022Article
- LEA motifs promote desiccation tolerance in vivo.BMC biology · 2021Article
- Modular Assembly of Ordered Hydrophilic Proteins Improve Salinity Tolerance inInternational journal of molecular sciences · 2021Article
- Late Embryogenesis Abundant Protein-Client Protein Interactions.Plants (Basel, Switzerland) · 2020Review
- Replica exchange molecular dynamics simulation study on the mechanism of desiccation-induced structuralization of an intrinsically disordered peptide as a model of LEA proteins.Biophysics and physicobiology · 2019Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
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Abstract
We tested whether a short model peptide derived from a group 3 late embryogenesis abundant (G3LEA) protein is able to maintain the fluorescence activity of a red fluorescent protein, mKate2, in the dry state. The fluorescence intensity of mKate2 alone decreased gradually through repeated dehydration-rehydration treatments. However, in the presence of the LEA model peptide, the peak intensity was maintained almost perfectly during such stress treatments, which implies that the three dimensional structure of the active site of mKate2 was protected even under severe desiccation conditions. For comparison, similar experiments were performed with other additives such as a native G3LEA protein, trehalose and BSA, all of whose protective abilities were lower than that of the LEA model peptide.
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