Association studies to transporting proteins of fac‑Re<sup>I</sup>(CO)<sub>3</sub>(pterin)(H<sub>2</sub>O) complex

A new synthetic route to acquire the water soluble complex fac-Re<sup>I</sup>(CO)<sub>3</sub>(pterin)(H<sub>2</sub>O) was carried out in aqueous solution. The complex has been obtained with success via the fac-[Re<sup>I</sup>(CO)<sub>3</sub>...

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Autores principales: Ragone, Fabricio, Martínez Saavedra, Héctor Hernando, García, Pablo F., Wolcan, Ezequiel, Argüello, Gerardo A., Ruiz, Gustavo Teodosio
Formato: Articulo
Lenguaje:Inglés
Publicado: 2017
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/105595
https://link.springer.com/article/10.1007%2Fs00775-016-1410-7
Aporte de:
id I19-R120-10915-105595
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Física
Química
rhenium(I) complex
serum albumins
binding study
fluorescence quenching
circular dichroism
thermodynamic parameters
spellingShingle Ciencias Exactas
Física
Química
rhenium(I) complex
serum albumins
binding study
fluorescence quenching
circular dichroism
thermodynamic parameters
Ragone, Fabricio
Martínez Saavedra, Héctor Hernando
García, Pablo F.
Wolcan, Ezequiel
Argüello, Gerardo A.
Ruiz, Gustavo Teodosio
Association studies to transporting proteins of fac‑Re<sup>I</sup>(CO)<sub>3</sub>(pterin)(H<sub>2</sub>O) complex
topic_facet Ciencias Exactas
Física
Química
rhenium(I) complex
serum albumins
binding study
fluorescence quenching
circular dichroism
thermodynamic parameters
description A new synthetic route to acquire the water soluble complex fac-Re<sup>I</sup>(CO)<sub>3</sub>(pterin)(H<sub>2</sub>O) was carried out in aqueous solution. The complex has been obtained with success via the fac-[Re<sup>I</sup>(CO)<sub>3</sub>(H<sub>2</sub>O)<sub>3</sub>]Cl precursor complex. Re<sup>I</sup>(CO)<sub>3</sub>(pterin)(H<sub>2</sub>O) has been found to bind strongly with bovine and human serum albumins (BSA and HSA) with intrinsic-binding constants, K<sub>b</sub>, of 6.5 × 10<sup>5</sup> M<sup>−1</sup> and 5.6 × 10<sup>5</sup> M<sup>−1</sup> at 310 K, respectively. The interactions of serum albumins with Re<sup>I</sup>(CO)<sub>3</sub>(pterin)(H<sub>2</sub>O) were evaluated employing UV–vis fluorescence and absorption spectroscopy and circular dichroism. The results suggest that the serum albumins-Re<sup>I</sup>(CO)<sub>3</sub>(pterin)(H<sub>2</sub>O) interactions occurred in the domain IIA-binding pocket without loss of helical stability of the proteins. The comparison of the fluorescence quenching of BSA and HSA due to the binding to the Re(I) complex suggested that local interaction around the Trp 214 residue had taken place. The analysis of the thermodynamic parameters ΔG<sup>0</sup>, ΔH<sup>0</sup>, and ΔS<sup>0</sup> indicated that the hydrophobic interactions played a major role in both HSA-Re(I) and BSA-Re(I) association processes. All these experimental results suggest that these proteins can be considered as good carriers for transportation of Re<sup>I</sup>(CO)<sub>3</sub>(pterin)(H<sub>2</sub>O) complex. This is of significant importance in relation to the use of this Re(I) complex in several biomedical fields, such as photodynamic therapy and radiopharmacy.
format Articulo
Articulo
author Ragone, Fabricio
Martínez Saavedra, Héctor Hernando
García, Pablo F.
Wolcan, Ezequiel
Argüello, Gerardo A.
Ruiz, Gustavo Teodosio
author_facet Ragone, Fabricio
Martínez Saavedra, Héctor Hernando
García, Pablo F.
Wolcan, Ezequiel
Argüello, Gerardo A.
Ruiz, Gustavo Teodosio
author_sort Ragone, Fabricio
title Association studies to transporting proteins of fac‑Re<sup>I</sup>(CO)<sub>3</sub>(pterin)(H<sub>2</sub>O) complex
title_short Association studies to transporting proteins of fac‑Re<sup>I</sup>(CO)<sub>3</sub>(pterin)(H<sub>2</sub>O) complex
title_full Association studies to transporting proteins of fac‑Re<sup>I</sup>(CO)<sub>3</sub>(pterin)(H<sub>2</sub>O) complex
title_fullStr Association studies to transporting proteins of fac‑Re<sup>I</sup>(CO)<sub>3</sub>(pterin)(H<sub>2</sub>O) complex
title_full_unstemmed Association studies to transporting proteins of fac‑Re<sup>I</sup>(CO)<sub>3</sub>(pterin)(H<sub>2</sub>O) complex
title_sort association studies to transporting proteins of fac‑re<sup>i</sup>(co)<sub>3</sub>(pterin)(h<sub>2</sub>o) complex
publishDate 2017
url http://sedici.unlp.edu.ar/handle/10915/105595
https://link.springer.com/article/10.1007%2Fs00775-016-1410-7
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