Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein

2013 ◽  
Vol 48 (8) ◽  
pp. i-i
Author(s):  
C. Santambrogio ◽  
F. Favretto ◽  
M. D'Onofrio ◽  
M. Assfalg ◽  
R. Grandori ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Fatty Acid ◽  
Ligand Binding ◽  
Human Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Nmr Analysis ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein

2013 ◽  
Vol 48 (8) ◽  
pp. 895-903 ◽  
Author(s):  
C. Santambrogio ◽  
F. Favretto ◽  
M. D'Onofrio ◽  
M. Assfalg ◽  
R. Grandori ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Fatty Acid ◽  
Ligand Binding ◽  
Human Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Nmr Analysis ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Ligand Binding Promiscuity of Human Liver Fatty Acid Binding Protein: Structural and Dynamic Insights from an Interaction Study with Glycocholate and Oleate

ChemBioChem ◽  
2013 ◽  
Vol 14 (14) ◽  
pp. 1807-1819 ◽  
Author(s):  
Filippo Favretto ◽  
Michael Assfalg ◽  
Mariana Gallo ◽  
Daniel Oscar Cicero ◽  
Mariapina D'Onofrio ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Ligand Binding ◽  
Human Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Interaction Study ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Human Liver Fatty Acid Binding Protein: Solution Structure and Ligand Binding

2009 ◽  
Vol 96 (3) ◽  
pp. 600a ◽  
Author(s):  
Jun Cai ◽  
Christian Lücker ◽  
Zhongjing Chen ◽  
Elena Klimtchuk ◽  
Ye Qiao ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Ligand Binding ◽  
Human Liver ◽  
Solution Structure ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Protein Solution ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Bile salt recognition by human liver fatty acid binding protein

FEBS Journal ◽  
2015 ◽  
Vol 282 (7) ◽  
pp. 1271-1288 ◽  
Author(s):  
Filippo Favretto ◽  
Carlo Santambrogio ◽  
Mariapina D'Onofrio ◽  
Henriette Molinari ◽  
Rita Grandori ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Bile Salt ◽  
Human Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Structural and functional interaction of fatty acids with human liver fatty acid-binding protein (L-FABP) T94A variant

FEBS Journal ◽  
2014 ◽  
Vol 281 (9) ◽  
pp. 2266-2283 ◽  
Author(s):  
Huan Huang ◽  
Avery L. McIntosh ◽  
Gregory G. Martin ◽  
Kerstin K. Landrock ◽  
Danilo Landrock ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Human Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Functional Interaction ◽  
Protein L ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

scholarly journals Effect on ligand binding of arginine mutations in recombinant rat liver fatty acid-binding protein

1994 ◽  
Vol 297 (1) ◽  
pp. 103-107 ◽  
Author(s):  
A E Thumser ◽  
C Evans ◽  
A F Worrall ◽  
D C Wilton
Keyword(s):  
Fatty Acid ◽  
Ligand Binding ◽  
Rat Liver ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Liver Fatty Acid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Wide Range ◽  
Arginine Residues

Rat liver fatty acid-binding protein is able to accommodate a wide range of non-polar anions in addition to long-chain fatty acids. The two arginine residues of rat liver fatty acid-binding protein, Arg122 and Arg126, have been mutated and the effect of mutation on ligand binding investigated. No significant decrease in affinity for the fluorescent fatty acid analogue, 11-(5-dimethylaminonaphthalenesulphonyl amino)undecanoic acid, or oleate was observed. However, the apparent affinity for oleoyl-CoA was slightly increased with the mutations Ala122 and Gln122 such that oleoyl-CoA rather than oleate became the preferred ligand for these mutants. Small changes in protein stability were observed with the Arg122 mutations. The lack of notable ionic involvement of the conserved internal residue Arg122 in ligand binding is consistent with the hypothesis that the mode of ligand binding in liver fatty acid-binding protein is markedly different from that of other members of this lipid-binding protein family.

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