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

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...

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Bibliographic Details
Published in:Prostaglandins, leukotrienes and essential fatty acids leukotrienes and essential fatty acids, 2015-02, Vol.93, p.37-43
Main Authors: Curto, LM, Angelani, CR, Delfino, JM
Format: Article
Language:English
Subjects:
Advanced Basic Science
Amyloid aggregation
Animals
Endocrinology & Metabolism
Fatty Acid-Binding Proteins - chemistry
Fatty Acid-Binding Proteins - metabolism
Folding
Intestinal Fatty Acid Binding Protein (IFABP)
Ligand binding
Ligands
Protein Multimerization
Protein Structure, Secondary
β-barrel proteins
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Summary: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.
ISSN:0952-3278
1532-2823
DOI:10.1016/j.plefa.2014.08.001