Ligand-Binding Proteins: Structure, Stability and Practical Application

Stepanenko, Olga V.; Fonin, Alexander V.; Stepanenko, Olesya V.; Kuznetsova, Irina М.; Turoverov, Konstantin К.

doi:10.5772/38013

Cited by 6 publications

(8 citation statements)

References 131 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Studies of the binding specificity of OBPs towards several common odorants, which were performed mostly with bovine OBP and porcine OBP-I (pOBP), have revealed that OBPs can bind a broad spectrum of hydrophobic molecules of medium size (Stepanenko et al 2012). The industrial application of these proteins in odour control or as general microcapsules is very appealing due to their broad specificity and their thermo-stability (up to 60°C or up to 65°C if in complex with a ligand) (Paolini et al 1999).…”

Section: Discussionmentioning

confidence: 99%

“…According to the literature, heterocyclic derivatives are among the ligands with the highest affinity for OBPs; thiazoles, terpenoids and their derivatives as well as mediumsized aliphatic alcohols and aldehydes also have good affinity for OBP (Stepanenko et al 2012). Spherically shaped terpenoids, such as camphor and its analogues, and polar compounds, such as the short-chain fatty acids, exhibit poor affinity to OBPs.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Odorant binding proteins: a biotechnological tool for odour control

Silva

Matamá

Azóia

et al. 2013

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

The application of an odorant binding protein for odour control and fragrance delayed release from a textile surface was first explored in this work. Pig OBP-1 gene was cloned and expressed in Escherichia coli, and the purified protein was biochemically characterized. The IC₅₀ values (concentrations of competitor that caused a decay of fluorescence to half-maximal intensity) were determined for four distinct fragrances, namely, citronellol, benzyl benzoate, citronellyl valerate and ethyl valerate. The results showed a strong binding of citronellyl valerate, citronellol and benzyl benzoate to the recombinant protein, while ethyl valerate displayed weaker binding. Cationized cotton substrates were coated with porcine odorant binding protein and tested for their capacity to retain citronellol and to mask the smell of cigarette smoke. The immobilized protein delayed the release of citronellol when compared to the untreated cotton. According to a blind evaluation of 30 assessors, the smell of cigarette smoke, trapped onto the fabrics' surface, was successfully attenuated by porcine odorant binding protein (more than 60 % identified the weakest smell intensity after protein exposure compared to β-cyclodextrin-treated and untreated cotton fabrics). This work demonstrated that porcine odorant binding protein can be an efficient solution to prevent and/or remove unpleasant odours trapped on the large surface of textiles. Its intrinsic properties make odorant binding proteins excellent candidates for controlled release systems which constitute a new application for this class of proteins.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Odorant binding proteins: a biotechnological tool for odour control

Silva

Matamá

Azóia

et al. 2013

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

show abstract

“…The extreme resistance to a variety of denaturing effects is a special feature of FPs. For example, they are approximately 1000 times more stable than proteins of the lipocalin superfamily (Stepanenko et al, 2012a). The structure of odorant-binding proteins (pOBP), which represents a β-barrel composed of eight β-strands with a central nonpolar cavity for the binding of hydrophobic odorant molecules, possesses stability that is close to that of the GFP-like proteins (the difference in the free energy of pOBP in the native and unfolded states in the absence of a denaturant is −25 kJ/mol).…”

Section: Pioneering Studies Of Fluorescent Protein Stabilitymentioning

confidence: 99%

Beta-Barrel Scaffold of Fluorescent Proteins

Stepanenko

Kuznetsova

Verkhusha

et al. 2013

International Review of Cell and Molecular Biology

View full text Add to dashboard Cite

This review focuses on the current view of the interaction between the β-barrel scaffold of fluorescent proteins and their unique chromophore located in the internal helix. The chromophore originates from the polypeptide chain and its properties are influenced by the surrounding protein matrix of the β-barrel. On the other hand, it appears that a chromophore tightens the β-barrel scaffold and plays a crucial role in its stability. Furthermore, the presence of a mature chromophore causes hysteresis of protein unfolding and refolding. We survey studies measuring protein unfolding and refolding using traditional methods as well as new approaches, such as mechanical unfolding and reassembly of truncated fluorescent proteins. We also analyze models of fluorescent protein unfolding and refolding obtained through different approaches, and compare the results of protein folding in vitro to co-translational folding of a newly synthesized polypeptide chain.

show abstract

“…The results obtained in this study have not only fundamental but also practical significance. As was already mentioned, PBPs are actively used in the development of the sensing elements of biosensor systems for the detection of various analytes [ 13 , 40 , 41 , 42 , 43 , 44 , 45 , 46 , 47 , 48 , 49 , 50 , 51 , 52 , 53 , 54 , 55 , 56 , 57 , 58 , 59 , 60 , 61 , 62 , 97 ]. In order for the biosensor system to continuously respond to changes in the concentration of the testing substance in an analyzed medium, the dissociation constant of a sensing element-analyte complex should correspond to the middle of the tested range of the analyte concentrations.…”

Section: Resultsmentioning

confidence: 99%

“…Periplasmic ligand-binding proteins (PBPs) are particularly interesting for studying functionally important structural changes in a protein molecule, since the conformations of the apo- and holo-forms of these proteins are typically rather different [ 11 , 12 ]. Proteins of this class are intermediary receptors of ABC transport systems and participate in the active transport of small soluble molecules (such as metal ions, amino acids, sugars, vitamins, and peptides) through cell membranes by hydrolysis of ATP [ 13 ]. PBPs consist of two domains connected by a hinge region, with an active center located within the cleft between the two domains [ 11 ].…”

Section: Introductionmentioning

confidence: 99%

Osmolyte-Like Stabilizing Effects of Low GdnHCl Concentrations on d-Glucose/d-Galactose-Binding Protein

Fonin

Golikova

Зверева

et al. 2017

IJMS

Self Cite

View full text Add to dashboard Cite

The ability of d-glucose/d-galactose-binding protein (GGBP) to reversibly interact with its ligands, glucose and galactose, makes this protein an attractive candidate for sensing elements of glucose biosensors. This potential is largely responsible for attracting researchers to study the conformational properties of this protein. Previously, we showed that an increase in the fluorescence intensity of the fluorescent dye 6-bromoacetyl-2-dimetylaminonaphtalene (BADAN) is linked to the holo-form of the GGBP/H152C mutant in solutions containing sub-denaturing concentrations of guanidine hydrochloride (GdnHCl). It was hypothesized that low GdnHCl concentrations might lead to compaction of the protein, thereby facilitating ligand binding. In this work, we utilize BADAN fluorescence spectroscopy, intrinsic protein UV fluorescence spectroscopy, and isothermal titration calorimetry (ITC) to show that the sub-denaturing GdnHCl concentrations possess osmolyte-like stabilizing effects on the structural dynamics, conformational stability, and functional activity of GGBP/H152C and the wild type of this protein (wtGGBP). Our data are consistent with the model where low GdnHCl concentrations promote a shift in the dynamic distribution of the protein molecules toward a conformational ensemble enriched in molecules with a tighter structure and a more closed conformation. This promotes the increase in the configurational complementarity between the protein and glucose molecules that leads to the increase in glucose affinity in both GGBP/H152C and wtGGBP.

show abstract

Ligand-Binding Proteins: Structure, Stability and Practical Application

Cited by 6 publications

References 131 publications

Odorant binding proteins: a biotechnological tool for odour control

Odorant binding proteins: a biotechnological tool for odour control

Beta-Barrel Scaffold of Fluorescent Proteins

Osmolyte-Like Stabilizing Effects of Low GdnHCl Concentrations on d-Glucose/d-Galactose-Binding Protein

Contact Info

Product

Resources

About