title: Investigation of charged polymer influence on green fluorescent protein thermal stability.
abstract: Methods of stabilization and formulation of proteins are important in both biopharmaceutical and biocatalysis industries. Polymers are often used as modifiers of characteristics of biological macromolecules to improve the biochemical activity and stability of proteins or drug bioavailability. Green fluorescent protein (GFP) shows remarkable structural stability and high fluorescence; its stability can be directly related to its fluorescence output, among other characteristics. GFP is stable under increasing temperatures, and its thermal denaturation is highly reproducible. Relative thermal stability was undertaken by incubation of GFP at varying temperatures and GFP fluorescence was used as a reporter for unfolding. At 80°C, DEAE-dextran did not have any effect on GFP fluorescence, indicating that it does not confer stability.
authors.affiliation: Department of Biochemical and Pharmaceutical Technology, School of Pharmaceutical Sciences, University of São Paulo, Av. Prof. Lineu Prestes, 580-Bloco 16, São Paulo, SP, 05508-900, Brazil. lclnovaes@usp.br
authors.forename: Letícia Celia
authors.initials: LC
authors.lastname: de Lencastre Novaes
authors.forename: Priscila Gava
authors.initials: PG
authors.lastname: Mazzola
authors.forename: Adalberto
authors.initials: A
authors.lastname: Pessoa
authors.forename: Thereza Christina
authors.initials: TC
authors.lastname: Vessoni Penna
mesh_terms: D049452:Green Fluorescent Proteins / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*; D011489:Protein Denaturation; D055672:Static Electricity; D013696:Temperature
chemical_list: D011108:Polymers; D049452:Green Fluorescent Proteins