Dimerization capacities of FGF2 purified with or without heparin-affinity chromatography (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Dimerization capacities of FGF2 purified with or without heparin-affinity chromatography (Articolo in rivista) (literal)

Anno

• 2014-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1371/journal.pone.0110055 (literal)

Alternative label

• Platonova N.; Miquel G.; Chiu L.-Y.; Taouji S.; Moroni E.; Colombo G.; Chevet E.; Sue S.-C.; Bikfalvi A. (2014)
  Dimerization capacities of FGF2 purified with or without heparin-affinity chromatography
  in PloS one
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Platonova N.; Miquel G.; Chiu L.-Y.; Taouji S.; Moroni E.; Colombo G.; Chevet E.; Sue S.-C.; Bikfalvi A. (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

• http://www.scopus.com/inward/record.url?eid=2-s2.0-84907829526&partnerID=q2rCbXpz (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 9 (literal)

Rivista

• PloS one (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 10 (literal)

Note

• Scopu (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• INSERM U1029, Allée Geoffroy St. Hilaire, Pessac, France; Université Bordeaux I, Allée Geoffroy St. Hilaire, Pessac, France; INSERM U1053, Team Avenir, Bordeaux, France; Institute of Bioinformatics and Structure Biology, National Tsing Hua University, Hsinchu, Taiwan; Istituto di Chimica del Riconoscimento Molecolare, CNR, I-Milano, Italy; Department of Health Sciences, University of Milan, San Paolo Hospital, Milan, Italy (literal)

Titolo

• Dimerization capacities of FGF2 purified with or without heparin-affinity chromatography (literal)

Abstract

• Fibroblast growth factor-2 (FGF2) is a pleiotropic growth factor exhibiting a variety of biological activities. In this article, we studied the capacity of FGF2 purified with or without heparin affinity chromatography to self-associate. Analyzing the NMR HSQC spectra for different FGF2 concentrations, heparin-affinity purified FGF2 showed perturbations that indicate dimerization and are a higher-order oligomerization state. HSQC perturbation observed with different FGF2 concentrations revealed a heparin-binding site and two dimer interfaces. Thus, with increasing protein concentrations, FGF2 monomers make contacts with each other and form dimers or higher order oligomers. On the contrary, FGF2 purified with ionexchange chromatography did not show similar perturbation indicating that self-association of FGF2 is eliminated if purification is done without heparin-affinity chromatography. The HSQC spectra of heparin-affinity purified FGF2 can be reproduced to some extent by adding heparin tetra-saccharide to ion exchange chromatography purified FGF2. Heparinaffinity purified FGF2 bound to acceptor and donor beads in a tagged form using His-tagged or GST-tagged proteins, also dimerized in the AlphaScreen TM assay. This assay was further validated using different experimental conditions and competitors. The assay constitutes an interesting tool to study dimerization of other FGF forms as well. (literal)

Prodotto di

• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)
• simulazioni molecolari di sistemi biologici (INT.P02.001.001) (Modulo)

Autore CNR

• ELISABETTA MORONI (Persona)
• GIORGIO COLOMBO (Unità di personale interno)

Incoming links:

Prodotto

• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)
• simulazioni molecolari di sistemi biologici (INT.P02.001.001) (Modulo)

Autore CNR di

• GIORGIO COLOMBO (Unità di personale interno)
• ELISABETTA MORONI (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• PloS one (Rivista)