Dataset of the construction and characterization of stable biological nanoparticles
This article shows the dataset of clearance assays and the reconstitution of stable biological nano-complexes using both detergent-assisted and spontaneous solubilization of phospholipids by the recombinant purified apolipoprotein A-I (apoA-I). Protein was intra-chain crosslinked in order to introdu...
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| Format: | Article |
| Language: | English |
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Elsevier
2020-12-01
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| Series: | Data in Brief |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340920314189 |
| _version_ | 1818921951473696768 |
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| author | Romina A. Gisonno M. Alejandra Tricerri Marina C. Gonzalez Horacio A. Garda Nahuel A. Ramella Ivo Díaz Ludovico |
| author_facet | Romina A. Gisonno M. Alejandra Tricerri Marina C. Gonzalez Horacio A. Garda Nahuel A. Ramella Ivo Díaz Ludovico |
| author_sort | Romina A. Gisonno |
| collection | DOAJ |
| description | This article shows the dataset of clearance assays and the reconstitution of stable biological nano-complexes using both detergent-assisted and spontaneous solubilization of phospholipids by the recombinant purified apolipoprotein A-I (apoA-I). Protein was intra-chain crosslinked in order to introduce steric constrains. Then, native and crosslinked protein function was evaluated by a data collection of dimiristoyl phosphatidyl choline (DMPC) micellization curves. Additionally, resulting particles from spontaneous or detergent-assisted lipid solubilization were characterized by transmission electron microscopy (TEM), size exclusion chromatography (SEC), and native polyacrylamide gel electrophoresis (PAGE). Here we set up an experimental design that may help study protein structure based on its function, since interaction with biological membranes and lipids is an intrinsic activity attributed to many proteins in circulation. In addition, by t-test analysis of collected-data, we examined the formation of lipoprotein particles by native and intra-chain crosslinked proteins under different conditions like temperature and time incubation. Thus, data shown here strengthen the usefulness of an easy, rapid, accessible and inexpensive approach to test protein flexibility related to its function. |
| first_indexed | 2024-12-20T01:45:48Z |
| format | Article |
| id | doaj.art-42227e38581a46d08e5c4cffc9d1d4f5 |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-12-20T01:45:48Z |
| publishDate | 2020-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-42227e38581a46d08e5c4cffc9d1d4f52022-12-21T19:57:46ZengElsevierData in Brief2352-34092020-12-0133106536Dataset of the construction and characterization of stable biological nanoparticlesRomina A. Gisonno0M. Alejandra Tricerri1Marina C. Gonzalez2Horacio A. Garda3Nahuel A. Ramella4Ivo Díaz Ludovico5Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), Argentina; Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Calle 60 y 120, La Plata CP 1900, ArgentinaInstituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), Argentina; Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Calle 60 y 120, La Plata CP 1900, ArgentinaInstituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), Argentina; Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Calle 60 y 120, La Plata CP 1900, ArgentinaInstituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), Argentina; Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Calle 60 y 120, La Plata CP 1900, ArgentinaInstituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), Argentina; Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Calle 60 y 120, La Plata CP 1900, Argentina; Corresponding authors at: Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), Argentina.Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), Argentina; Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Calle 60 y 120, La Plata CP 1900, Argentina; Corresponding authors at: Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), Argentina.This article shows the dataset of clearance assays and the reconstitution of stable biological nano-complexes using both detergent-assisted and spontaneous solubilization of phospholipids by the recombinant purified apolipoprotein A-I (apoA-I). Protein was intra-chain crosslinked in order to introduce steric constrains. Then, native and crosslinked protein function was evaluated by a data collection of dimiristoyl phosphatidyl choline (DMPC) micellization curves. Additionally, resulting particles from spontaneous or detergent-assisted lipid solubilization were characterized by transmission electron microscopy (TEM), size exclusion chromatography (SEC), and native polyacrylamide gel electrophoresis (PAGE). Here we set up an experimental design that may help study protein structure based on its function, since interaction with biological membranes and lipids is an intrinsic activity attributed to many proteins in circulation. In addition, by t-test analysis of collected-data, we examined the formation of lipoprotein particles by native and intra-chain crosslinked proteins under different conditions like temperature and time incubation. Thus, data shown here strengthen the usefulness of an easy, rapid, accessible and inexpensive approach to test protein flexibility related to its function.http://www.sciencedirect.com/science/article/pii/S2352340920314189Apolipoprotein A-IBS3 crosslinkerLipid-bindingGradient gel electrophoresisNanoparticles |
| spellingShingle | Romina A. Gisonno M. Alejandra Tricerri Marina C. Gonzalez Horacio A. Garda Nahuel A. Ramella Ivo Díaz Ludovico Dataset of the construction and characterization of stable biological nanoparticles Data in Brief Apolipoprotein A-I BS3 crosslinker Lipid-binding Gradient gel electrophoresis Nanoparticles |
| title | Dataset of the construction and characterization of stable biological nanoparticles |
| title_full | Dataset of the construction and characterization of stable biological nanoparticles |
| title_fullStr | Dataset of the construction and characterization of stable biological nanoparticles |
| title_full_unstemmed | Dataset of the construction and characterization of stable biological nanoparticles |
| title_short | Dataset of the construction and characterization of stable biological nanoparticles |
| title_sort | dataset of the construction and characterization of stable biological nanoparticles |
| topic | Apolipoprotein A-I BS3 crosslinker Lipid-binding Gradient gel electrophoresis Nanoparticles |
| url | http://www.sciencedirect.com/science/article/pii/S2352340920314189 |
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