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Artículo

Toward a common aggregation mechanism for a β-barrel protein family: insights derived from a stable dimeric species

Angelani, Carla RominaIcon ; Curto, Lucrecia MaríaIcon ; Cabanas, Inés S; Caramelo, Julio JavierIcon ; Uversky, Vladimir N; Delfino, Jose MariaIcon
Fecha de publicación: 09/2014
Editorial: Elsevier Science
Revista: Biochimica Et Biophysica Acta-proteins And Proteomics
ISSN: 1570-9639
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:
Bioquímica y Biología Molecular

Resumen

Δ78Δ is a second generation functional all-β sheet variant of IFABP (intestinal fatty acid binding protein) corresponding to the fragment 29-106 of the parent protein. This protein and its predecessor, Δ98Δ (segment 29-126 of IFABP), were initially uncovered by controlled proteolysis. Remarkably, although IFABP and Δ98Δ are monomers in solution, Δ78Δ adopts a stable dimeric structure. With the aim of identifying key structural features that modulate the aggregation of β-proteins, we evaluate here the structure and aggregation propensity of Δ78Δ. The 2,2,2-trifluoroethanol (TFE) induced aggregation of this protein shows a primary nucleation-elongation mechanism, characterized by the stabilization of a dimeric nucleus. Its rate of production from the co-solvent induced aggregation prone state governs the kinetics of polymerization. In this context, the value of Δ78Δ lies in the fact that - being a stable dimeric species - it reduces an otherwise bimolecular reaction to a unimolecular one. Interestingly, even though Δ78Δ and IFABP display similar conformational stability, the abrogated form of IFABP shows an enhanced aggregation rate, revealing the ancillary role played on this process by the free energy of the native proteins. Δ78Δ share with IFABP and Δ98Δ a common putative aggregation-prone central peptide. Differences in the exposure/accessibility of this segment dictated by the environment around this region might underlie the observed variations in the speed of aggregation. Lessons learnt from this natural dimeric protein might shed light on the early conformational events leading to β-conversion from barrels to amyloid aggregates.
Palabras clave: Fabp , Amiloide
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Atribución-NoComercial-SinDerivadas 2.5 Argentina (CC BY-NC-ND 2.5 AR)
Identificadores
URI: http://hdl.handle.net/11336/8480
URL: http://www.sciencedirect.com/science/article/pii/S1570963914001514
DOI: http://dx.doi.org/10.1016/j.bbapap.2014.06.002
Colecciones
Articulos(IIBBA)
Articulos de INST.DE INVEST.BIOQUIMICAS DE BS.AS(I)
Articulos(IQUIFIB)
Articulos de INST.DE QUIMICA Y FISICO-QUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Citación
Angelani, Carla Romina; Curto, Lucrecia María; Cabanas, Inés S; Caramelo, Julio Javier; Uversky, Vladimir N; et al.; Toward a common aggregation mechanism for a β-barrel protein family: insights derived from a stable dimeric species; Elsevier Science; Biochimica Et Biophysica Acta-proteins And Proteomics; 1844; 9; 9-2014; 1599-1607
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