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Artículo

Structural coalescence underlies the aggregation propensity of a β-barrel protein motif

Angelani, Carla RominaIcon ; Caramelo, Julio JavierIcon ; Curto, Lucrecia MaríaIcon ; Delfino, Jose MariaIcon
Fecha de publicación: 02/2017
Editorial: Public Library of Science
Revista: Plos One
ISSN: 1932-6203
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:
Otras Ciencias Biológicas

Resumen

A clear understanding of the structural foundations underlying protein aggregation is an elusive goal of central biomedical importance. A step toward this aim is exemplified by the β- barrel motif represented by the intestinal fatty acid binding protein (IFABP) and two abridged all-β sheet forms (δ98δ and δ78δ). At odds with the established notion that a perturbation of the native fold should necessarily favor a buildup of intermediate forms with an enhanced tendency to aggregate, the intrinsic stability (δG°H2O) of these proteins does not bear a straightforward correlation with their trifluoroethanol (TFE)-induced aggregation propensity. In view of this fact, we found it more insightful to delve into the connection between structure and stability under sub-aggregating conditions (10% TFE). In the absence of the co-solvent, the abridged variants display a common native-like region decorated with a disordered Cterminal stretch. Upon TFE addition, an increase in secondary structure content is observed, assimilating them to the parent protein. In this sense, TFE perturbs a common native like region while exerting a global compaction effect. Importantly, in all cases, fatty acid binding function is preserved. Interestingly, energetic as well as structural diversity in aqueous solution evolves into a common conformational ensemble more akin in stability. These facts reconcile apparent paradoxical findings related to stability and rates of aggregation. This scenario likely mimics the accrual of aggregation-prone species in the population, an early critical event for the development of fibrillation.
Palabras clave: Amyloid Aggregation , Fatty Acid Binding Protein , Beta Barrel , Structural Coalescence
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution 2.5 Unported (CC BY 2.5)
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URI: http://hdl.handle.net/11336/47224
DOI: http://dx.doi.org/10.1371/journal.pone.0170607
URL: http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0170607
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Articulos(IQUIFIB) [586]
Articulos de INST.DE QUIMICA Y FISICO-QUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Citación
Angelani, Carla Romina; Caramelo, Julio Javier; Curto, Lucrecia María; Delfino, Jose Maria; Structural coalescence underlies the aggregation propensity of a β-barrel protein motif; Public Library of Science; Plos One; 12; 2; 2-2017; 1-20; e0170607
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