Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity

Curto, Lucrecia María
Angelani, Carla Romina
Delfino, Jose Maria

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Publication date

February 2015

DOI

10.1016/j.plefa.2014.08.001

Publisher

Elsevier BV

ISSN

0952-3278

Journal

Prostaglandins Leukotrienes and Essential Fatty Acids

Citation count (estimate)

Abstract

Natural β-folds manage to fold up successfully. By contrast, attempts to dissect fragments or peptides from well folded β-sheet proteins have met with insurmountable difficulties. Here we briefly review selected successful cases of intervention on the well-known scaffold of intestinal fatty acid binding protein (IFABP). Lessons from these examples might set guidelines along the design of proteins belonging to this class. Impact of modifications on topology, binding and aggregation is highlighted. With the aid of abridged variants of IFABP we focus on key structural features responsible for the assembly into oligomeric forms or aggregates.Fil: Curto, Lucrecia María. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coord...

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Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity

Abstract

Extracted data

Intervening in the β-barrel structure of lipid binding proteins: Consequences on folding, ligand-binding and aggregation propensity

Abstract

Extracted data

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