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Last update 08 May 2025

FABP6

Last update 08 May 2025

Basic Info

Synonyms

FABP6, fatty acid binding protein 6, fatty acid binding protein 6, ileal

+ [15]

Introduction

Binds to bile acids and is involved in enterohepatic bile acid metabolism. Required for efficient apical to basolateral transport of conjugated bile acids in ileal enterocytes (By similarity). In vitro binds to bile acids in the order: deoxycholic acid > cholic acid > chenodeoxycholic acid and respective BA conjugation modifies affinities in the order taurine-conjugated > glycine-conjugated > unconjugated bile acids. Stimulates gastric acid and pepsinogen secretion (By similarity). Essential for the survival of colon cancer cells to bile acid-induced apoptosis.

Drugs associated with FABP6

Colesevelam Hydrochloride

Target

FABP6

Mechanism

FABP6 modulators

Active Org.

CHEPLAPHARM Arzneimittel GmbH [+2]

Originator Org.

Genzyme Corp.

Active Indication

Diabetes Mellitus, Type 2 [+3]

Inactive Indication

Diabetes Mellitus, Noninsulin-Dependent, 2 [+1]

Drug Highest PhaseApproved

First Approval Ctry. / Loc.

United States

First Approval Date26 May 2000

HBS-107

Target

FABP6

Mechanism

FABP6 modulators

Active Org.-

Originator Org.

Hisamitsu Pharmaceutical Co., Inc.

Active Indication-

Inactive Indication

Hypercholesterolemia

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

DMP-504

Target

FABP6

Mechanism

FABP6 modulators

Active Org.-

Originator Org.

Bristol Myers Squibb Co.

Active Indication-

Inactive Indication

Hypercholesterolemia

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with FABP6

ISRCTN68585853

/ RecruitingPhase 2

A randomised, double-blind, multicentre, international placebo-controlled phase II study aimed at investigating the efficacy and safety of a novel modified-release tablet formulation of colesevelam hydrochloride in patients with idiopathic bile acid diarrhoea

Start Date16 Dec 2024

Sponsor / Collaborator

Cosmo Technologies Ltd.

NCT06197763

/ Not yet recruitingPhase 1/2IIT

Impact of Therapy Using Colesevelam Treatment Reducing Bile Acids in Patients With Fontan Circulation (MYSTIC) Pilot Study.

This is the first pilot study proposing a novel therapeutic option treating patients with Fontan circulation (FC), a high-risk condition that has no definite treatment options available, other than heart or heart-liver transplantation. The investigator's identification of elevated BA and their association with adverse clinical - investigational features in Fontan patients are novel.

Start Date01 Jun 2024

Sponsor / Collaborator

St. Boniface Hospital

NCT06925997

/ RecruitingEarly Phase 1IIT

Metabolic Effects of Endogenous Bile Acids After Gastric Bypass Surgery

Non-randomized, open-label, parallel-group clinical study evaluating the effects of endogenous bile acids on changes in plasma fibroblast growth factor-19 (FGF-19) and glucose metabolism by extended depletion of circulating bile acids using colesevelam as an experimental tool in subjects operated with gastric by-pass (RYGB).

Start Date02 May 2024

Sponsor / Collaborator

Hvidovre University Hospital

100 Clinical Results associated with FABP6

100 Translational Medicine associated with FABP6

0 Patents (Medical) associated with FABP6

354

Literatures (Medical) associated with FABP6

01 Jun 2025·Fish & Shellfish Immunology

Biochemical characterization and antibacterial activity of lipopolysaccharide binding proteins of the jellyfish Aurelia aurita and Rhopilema asamushi

Article

Author: Naberezhnykh, Gennadii ; Yuferova, Аleksandra ; Bakholdina, Svetlana ; Solov'eva, Tamara

Proteins capable of binding lipopolysaccharides (LPSs) of Gram-negative bacteria were isolated from the jellyfish of the Sea of Japan. LPS-binding proteins (ILBP - invertebrate lipopolysaccharide-binding proteins) were found in lysates of the jellyfish mesogloea by immunofluorescence assay with fluorescein-labeled LPS (F-LPS). Cation exchange chromatography was used isolate and purify ILBPs from jellyfish lysate. Fractions of jellyfish lysate after cation exchange chromatography were shown to contain high-molecular-weight ILBPs. By ligand enzyme solid phase assay it was shown that isolated ILBP of jellyfishes was bound to LPS directly by concentration-dependent manner in saturation process. The Scatchard analysis plot of the binding data gave a biphasic curve, suggesting that there were two types of independent binding sites in ILBP. Both isolated R-LPS and free lipid A inhibited binding of LBP with B LPS. The O-specific side chain of LPS was not involved in the interaction with ILBP. This suggested that the binding proteins recognized the core oligosaccharide and the lipid A portion of LPS. The disaggregation of various forms of LPS upon interaction with ILBPs from two species of jellyfish was also studied by dynamic light scattering (DLS). The distribution pattern and particle size (34 nm and 88.8 nm) of R-LPS in complex with ILBP from R. asamushi indicate disaggregation of R-LPS. The negative charge of Rd-LPS (-42.2 mV) in the LPS-ILBP-Ropilema complex is neutralized to -4.4 mV. It was shown that the ILBP was involved in the defense mechanism of the jellyfish by agglutinating the Gram-negative bacteria Escherichia coli and Yersinia pseudotuberculosis. We studied the effects of ILBP concentration on the permeability of bacterial walls. Responses to ILBP varied across the studied Gram-negative bacteria. Y. pseudotuberculosis was more tolerant to the effects of ILBP compared to E. coli K-12. We attributed the observed distinctions to the different structure of LPSs. E. coli K-12 contains LPS with short carbohydrate chains, and lipid A is more easily available for binding to ILBP. These invertebrate species are abundant and are of interest as new sources of LPS binding proteins for potential antimicrobial agents. Proteins modulating the biological activity of endotoxin are important not only because they provide insights into the mechanisms of host defense against Gram-negative bacteria but also because they may suggest new therapeutic approaches to control the deleterious effects of endotoxins.

01 Jun 2025·Journal of Structural Biology

Determinants of site-selectivity in human ileal bile acid-binding protein by NMR dynamic analysis of a functionally-impaired mutant

Article

Author: Horváth, Gergő ; Teski, Tamara ; Toke, Orsolya

Human ileal bile acid-binding protein (hI-BABP), a member of the family of intracellular lipid-binding proteins, has a key role in the enterohepatic circulation of bile salts. The two internal binding sites of hI-BABP exhibit positive cooperativity accompanied by a site preference of glycocholate (GCA) and glycochenodeoxycholate (GCDA), the two most abundant bile salts in the human body. Previous study of Q51A hI-BABP in its apo state, a mutant with lost site-selectivity, suggests that disruption of the hydrogen-bonding network in the vicinity of the C/D-turn has long-range dynamic effects. To improve our understanding of the determinants of site-selectivity in hI-BABP, a comparative NMR chemical shift and spin relaxation analysis of homo- and heterotypic bile salt complexes of wild-type and Q51A hI-BABP was carried out. The wild-type GCDA-complex shows a striking similarity with the thermodynamically most stable hI-BABP:GCDA:GCA complex in terms of both structure and dynamic behaviour, suggesting that the bound GCDA at site 1 has a decisive role in conveying key stabilizing interactions in the physiologically most abundant heterotypic complex. Destabilization of hI-BABP-GCDA by the functionally impairing mutation Q51A is indicated by both the increase of ms-timescale motions in key segments of the protein as well as by increased ps-ns local fluctuations superimposed on slow motions. Our study suggests that binding interactions in hI-BABP might be modulated by altering the dynamic behaviour of specific segments in the protein with implications for targeting the intracellular trafficking of bile salts and bile salt-induced stimulation of nuclear receptors.

01 Jan 2025·Protein Science

Structural dynamics and binding of Caenorhabditis elegans lifespan‐extending lipid binding protein‐3 to polyunsaturated fatty acids

Article

Author: Ortlund, Eric A. ; Wang, Meng C. ; Tillman, Matthew C. ; Cuevas, André R.

AbstractIntracellular lipid binding proteins (iLBPs) play crucial roles in lipid transport and cellular metabolism across the animal kingdom. Recently, a fat‐to‐neuron axis was described in Caenorhabditis elegans, in which lysosomal activity in the fat liberates polyunsaturated fatty acids (PUFAs) that signal to neurons and extend lifespan with durable fecundity. In this study, we investigate the structure and binding mechanisms of a lifespan‐extending lipid chaperone, lipid binding protein‐3 (LBP‐3), which shuttles dihomo‐γ‐linolenic (DGLA) acid from intestinal fat to neurons. We present the first high‐resolution crystal structure of LBP‐3, which reveals a classic iLBP fold with an unexpected and unique homodimeric arrangement via interstrand interactions that is incompatible with ligand binding. We identify key ionic interactions that mediate DGLA binding within the lipid binding pocket. Molecular dynamics simulations further elucidate LBP‐3's preferential binding to DGLA due to its rotational freedom and access to favorable binding conformations compared to other 20‐carbon PUFAs. We also propose that LBP‐3 dimerization may be a unique regulatory mechanism for lipid chaperones.

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FABP6

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