scholarly journals Deciphering Aspartyl Peptide Sweeteners Using the Ultimate Molecular Theory of Sweet Taste

2021 ◽  
Author(s):  
Huazhong He
Keyword(s):  
Hydrogen Bond ◽  
Bitter Taste ◽  
Sweet Taste ◽  
Hydrogen Donor ◽  
Helical Structures ◽  
Hydrogen Acceptor ◽  
Recognition Theory ◽  
Selection For ◽  
First Time ◽  
Alpha Carbon

More than thirty years ago, I proposed a theory about sweet and bitter molecules’ recognition by protein helical structures. Unfortunately the papers<br>could not go to public platform until now. The sweet and bitter taste theory is updated and presented in separated papers. 1,2 Under the guidance of the sweet<br>receptor helix recognition theory 1, aspartyl/aminomalonyl peptide sweeteners are deciphered. Here it demonstrates that, this series of sweeteners has a<br>hydrogen-bond type hydrogen donor - hydrogen acceptor DH-B moiety and their DH-B is very special. Their B of the DH-B moiety is an oxygen of the carboxylic<br>group, which is widely accepted one. The DH of the DH-B moiety however is the NH of the aspartyl/aminomalonyl peptide, which is a selection for the first time to<br>the best of my knowledge. Even more unusual, their dynamic action acts through<br>the hydrogen on alpha carbon of aspartyl/aminomalonyl group. The receptor main and side grooves have different space characteristics in accepting sweet<br>molecules’ groups, which is elaborated in this paper. This unprecedented elucidation well explains the aspartyl/aminomalonyl peptide sweeteners’<br>phenomenon and, in return, strongly supports this sweet receptor helix recognition theory.

scholarly journals Deciphering Aspartyl Peptide Sweeteners Using the Ultimate Molecular Theory of Sweet Taste

2021 ◽  
Author(s):  
Huazhong He
Keyword(s):  
Hydrogen Bond ◽  
Bitter Taste ◽  
Sweet Taste ◽  
Hydrogen Donor ◽  
Helical Structures ◽  
Hydrogen Acceptor ◽  
Recognition Theory ◽  
Selection For ◽  
First Time ◽  
Alpha Carbon

More than thirty years ago, I proposed a theory about sweet and bitter molecules’ recognition by protein helical structures. Unfortunately the papers<br>could not go to public platform until now. The sweet and bitter taste theory is updated and presented in separated papers. 1,2 Under the guidance of the sweet<br>receptor helix recognition theory 1, aspartyl/aminomalonyl peptide sweeteners are deciphered. Here it demonstrates that, this series of sweeteners has a<br>hydrogen-bond type hydrogen donor - hydrogen acceptor DH-B moiety and their DH-B is very special. Their B of the DH-B moiety is an oxygen of the carboxylic<br>group, which is widely accepted one. The DH of the DH-B moiety however is the NH of the aspartyl/aminomalonyl peptide, which is a selection for the first time to<br>the best of my knowledge. Even more unusual, their dynamic action acts through<br>the hydrogen on alpha carbon of aspartyl/aminomalonyl group. The receptor main and side grooves have different space characteristics in accepting sweet<br>molecules’ groups, which is elaborated in this paper. This unprecedented elucidation well explains the aspartyl/aminomalonyl peptide sweeteners’<br>phenomenon and, in return, strongly supports this sweet receptor helix recognition theory.

scholarly journals Ultimate Molecular Theory of Sweet Taste

2021 ◽  
Author(s):  
Huazhong He
Keyword(s):  
Binding Sites ◽  
Bitter Taste ◽  
Sweet Taste ◽  
Receptor Protein ◽  
Helical Structures ◽  
Hydrogen Acceptor ◽  
Bond Type ◽  
Multiple Binding Sites ◽  
Multiple Receptors ◽  
Multiple Binding

Abstract More than thirty years ago, I proposed a theory about sweet and bitter molecules’ recognition by protein helical structures. Unfortunately the papers could not go to public platform until now. The sweet and bitter taste theory is updated and presented in separated papers1,2. The sweet taste theory conveys that sweet molecules are recognized by receptor protein helical structures and the recognition process is a dynamic action, in which the sweet receptor protein helix has a torsion-spring-like oscillation between helical structures of 3.6 and 3 amino acids per turn. To help this kind of oscillation, there are two kinds of hydrogen donor and hydrogen acceptor DH-B entities for both receptor and sweet molecules: H-bond or non-H-bond. The distances between DH and B could be up to ~ 8.5 Å. The receptor H-bond type DH-B entities are the NH-O pairs forming H-bonds in protein helices; the receptor non-H-bond type DH-B entities are the ones from two pairs of NH-Os forming H-bonds which are about one turn away. To facilitate this kind of movement, the interaction of DH-Bs of a sweet molecule with those of sweet receptor, through a pair of complementary hydrogen bonds, must have hydrogen bond complementarities, which means Hbond type of ligands’ DH-Bs reacts on non-H-bond type of receptor’s O-NHs, and vice versa. As the oscillation may have different extent, it translates to sweet intensity. As recognition sites are only associated with a small fraction – helix structure of whole sweet receptor, multiple binding sites or multiple receptors are well expected.

scholarly journals Ultimate Molecular Theory of Sweet Taste

2021 ◽  
Author(s):  
Huazhong He
Keyword(s):  
Binding Sites ◽  
Bitter Taste ◽  
Sweet Taste ◽  
Receptor Protein ◽  
Helical Structures ◽  
Hydrogen Acceptor ◽  
Bond Type ◽  
Multiple Binding Sites ◽  
Multiple Receptors ◽  
Multiple Binding

Abstract More than thirty years ago, I proposed a theory about sweet and bittermolecules’ recognition by protein helical structures. Unfortunately the paperscould not go to public platform until now. The sweet and bitter taste theory isupdated and presented in separated papers1,2. The sweet taste theory conveysthat sweet molecules are recognized by receptor protein helical structures andthe recognition process is a dynamic action, in which the sweet receptor proteinhelix has a torsion-spring-like oscillation between helical structures of 3.6 and 3amino acids per turn. To help this kind of oscillation, there are two kinds ofhydrogen donor and hydrogen acceptor DH-B entities for both receptor andsweet molecules: H-bond or non-H-bond. The distances between DH and Bcould be up to ~ 8.5 Å. The receptor H-bond type DH-B entities are the NH-Opairs forming H-bonds in protein helices; the receptor non-H-bond type DH-Bentities are the ones from two pairs of NH-Os forming H-bonds which are aboutone turn away. To facilitate this kind of movement, the interaction of DH-Bs of asweet molecule with those of sweet receptor, through a pair of complementaryhydrogen bonds, must have hydrogen bond complementarities, which means Hbondtype of ligands’ DH-Bs reacts on non-H-bond type of receptor’s O-NHs, andvice versa. As the oscillation may have different extent, it translates to sweetintensity. As recognition sites are only associated with a small fraction – helixstructure of whole sweet receptor, multiple binding sites or multiple receptors arewell expected.

scholarly journals Ultimate Molecular Theory of Bitter Taste

2021 ◽  
Author(s):  
Huazhong He
Keyword(s):  
Binding Sites ◽  
Bitter Taste ◽  
Taste Receptor ◽  
Sweet Taste ◽  
Receptor Protein ◽  
Helical Structures ◽  
Sweet Taste Receptor ◽  
Multiple Binding Sites ◽  
Multiple Receptors ◽  
Multiple Binding

More than thirty years ago, I proposed a theory about sweet and bitter molecules’ recognition by protein helical structures. Unfortunately the papers could not go to public platform until now. Inspired by the sweet taste theory<sup>1,2</sup>, this bitter taste theory conveys that bitter molecules are recognized by receptor protein helical structures. The recognition process is a dynamic action, in which the receptor protein helices have a torsion-spring-like oscillation between helical structures of 3.6 and 4 amino acids per turn. Based on the characteristics of the bitter receptor protein helix oscillation, it perfectly explains why in bitter molecules, only one unit of hydrogen donor (DH) or hydrogen acceptor (B) is enough in helping molecules to elicit bitter taste. The potential DH and B in bitter receptor are any NH or O of receptor’s peptide NHs and Os, which are the ones forming intramolecular H-bonds responsible for the formation of receptor protein helical structures. Furthermore, only one unit of DH or B is allowed for structurally simple ligands. As recognition sites are only associated with a small fraction – helix structure of whole bitter receptor, multiple binding sites or multiple receptors are well expected. As the oscillation may have different extent, it translates to bitterness intensity. According to ligand-receptor binding motion, bitter receptor could be divided into two kinds of spaces, which are similar to the situation in sweet taste receptor: main and side grooves. These have been discussed in context and especially great details in paper titled deciphering aspartyl peptide sweeteners <sup>2</sup>.

scholarly journals Ultimate Molecular Theory of Bitter Taste

2021 ◽  
Author(s):  
Huazhong He
Keyword(s):  
Binding Sites ◽  
Bitter Taste ◽  
Taste Receptor ◽  
Sweet Taste ◽  
Receptor Protein ◽  
Helical Structures ◽  
Sweet Taste Receptor ◽  
Multiple Binding Sites ◽  
Multiple Receptors ◽  
Multiple Binding

More than thirty years ago, I proposed a theory about sweet and bitter molecules’ recognition by protein helical structures. Unfortunately the papers could not go to public platform until now. Inspired by the sweet taste theory<sup>1,2</sup>, this bitter taste theory conveys that bitter molecules are recognized by receptor protein helical structures. The recognition process is a dynamic action, in which the receptor protein helices have a torsion-spring-like oscillation between helical structures of 3.6 and 4 amino acids per turn. Based on the characteristics of the bitter receptor protein helix oscillation, it perfectly explains why in bitter molecules, only one unit of hydrogen donor (DH) or hydrogen acceptor (B) is enough in helping molecules to elicit bitter taste. The potential DH and B in bitter receptor are any NH or O of receptor’s peptide NHs and Os, which are the ones forming intramolecular H-bonds responsible for the formation of receptor protein helical structures. Furthermore, only one unit of DH or B is allowed for structurally simple ligands. As recognition sites are only associated with a small fraction – helix structure of whole bitter receptor, multiple binding sites or multiple receptors are well expected. As the oscillation may have different extent, it translates to bitterness intensity. According to ligand-receptor binding motion, bitter receptor could be divided into two kinds of spaces, which are similar to the situation in sweet taste receptor: main and side grooves. These have been discussed in context and especially great details in paper titled deciphering aspartyl peptide sweeteners <sup>2</sup>.

Interaction of Gold Atom with Clusters of Water: Few Computational Mise-En-Scènes with Hydrogen Bonding Motif

2008 ◽  
Vol 73 (11) ◽  
pp. 1457-1474 ◽  
Author(s):  
Eugene S. Kryachko
Keyword(s):  
Hydrogen Bond ◽  
Hydrogen Bonding ◽  
Computational Model ◽  
Photoelectron Spectroscopy ◽  
Water Clusters ◽  
Gold Atom ◽  
Proton Acceptor ◽  
Anion Photoelectron Spectroscopy ◽  
Relationship Of ◽  
First Time

The present work outlines the fair relationship of the computational model with the experiments on anion photoelectron spectroscopy for the gold-water complexes [Au(H2O)1≤n≤2]- that is established between the auride anion Au- and water monomer and dimer thanks to the nonconventional hydrogen bond where Au- casts as the nonconventional proton acceptor. This work also extends the computational model to the larger complexes [Au(H2O)3≤n≤5]- where gold considerably thwarts the shape of water clusters and even particularly breaks their conventional hydrogen bonding patterns. The fascinating phenomenon of the lavish proton acceptor character of Au- to form at least six hydrogen bonds with molecules of water is computationally unveiled in the present work for the first time.

scholarly journals The Sensory Quality and the Textural Properties of Functional Oolong Tea-Infused Set Type Yoghurt with Inulin

Foods ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1242
Author(s):  
Katarzyna Świąder ◽  
Anna Florowska ◽  
Zuzanna Konisiewicz
Keyword(s):  
Sensory Quality ◽  
Bitter Taste ◽  
Profile Analysis ◽  
Textural Properties ◽  
Sweet Taste ◽  
Oolong Tea ◽  
Quantitative Descriptive ◽  
Semi Solid ◽  
Positive Effect

Set type yoghurts are characterised by a semi-solid texture, which is created during the fermentation process. The tea infusion in this type of yoghurt production can influence the quality of the final product. Therefore, the aim of the experiment was to evaluate the influence of the addition of 3, 6 and 9% inulin to oolong tea-infused yoghurts on the sensory quality. It has been evaluated by trained experts using a Quantitative Descriptive Profile analysis and by consumers using hedonic scaling, as well as on instrumentally evaluated features such as texture, stability and visual parameters. The addition of oolong tea to yoghurt resulted in positive changes in the perception of sweet, peach and nectar odours and flavours, and also creaminess, as well as negative changes in the presence of a bitter taste, the whey presence and a colour intensification towards dark cream (p ≤ 0.05). The addition of inulin to the tested oolong tea yogurts caused a decrease in the whey presence and brightened the yoghurt’s colour (6% and 9%, p ≤ 0.05, respectively), as well as an improved creaminess and an increase in the sweet taste of the yoghurt. It was also observed that the addition of oolong tea deteriorated the instrumentally evaluated texture of the set yoghurts, while inulin at a higher concentration (9%, p ≤ 0.05) increased the firmness and adhesiveness. Moreover, the addition of inulin also had a positive effect on the yoghurt’s stability. The addition of inulin to oolong tea-infused set yoghurts may be valuable both as a source of prebiotic fibre in functional products and as a factor improving the quality of these products.

Rapid kinetics of second messenger production in bitter taste

1996 ◽  
Vol 270 (3) ◽  
pp. C926-C931 ◽  
Author(s):  
A. I. Spielman ◽  
H. Nagai ◽  
G. Sunavala ◽  
M. Dasso ◽  
H. Breer ◽  
...  
Keyword(s):  
Bitter Taste ◽  
Second Messengers ◽  
Second Messenger ◽  
Mouse Strains ◽  
Protective Mechanism ◽  
Transient Nature ◽  
Sucrose Octaacetate ◽  
Rapid Kinetics ◽  
First Time

The tasting of bitter compounds may have evolved as a protective mechanism against ingestion of potentially harmful substances. We have identified second messengers involved in bitter taste and show here for the first time that they are rapid and transient. Using a quench-flow system, we have studied bitter taste signal transduction in a pair of mouse strains that differ in their ability to taste the bitter stimulus sucrose octaacetate (SOA); however, both strains taste the bitter agent denatonium. In both strains of mice, denatonium (10 mM) induced a transient and rapid increase in levels of the second messenger inositol 1,4,5-trisphosphate (IP3) with a maximal production near 75-100 ms after stimulation. In contrast, SOA (100 microM) brought about a similar increase in IP3 only in SOA-taster mice. The response to SOA was potentiated in the presence of GTP (1 microM). The GTP-enhanced SOA-response supports a G protein-mediated response for this bitter compound. The rapid kinetics, transient nature, and specificity of the bitter taste stimulus-induced IP3 formation are consistent with the role of IP3 as a second messenger in the chemoelectrical transduction of bitter taste.

A single-round selection of selective DNA aptamers for mammalian cells by polymer-enhanced capillary transient isotachophoresis

The Analyst ◽  
2017 ◽  
Vol 142 (21) ◽  
pp. 4030-4038 ◽  
Author(s):  
Kazuki Hirose ◽  
Maho Tsuchida ◽  
Hinako Asakura ◽  
Koji Wakui ◽  
Keitaro Yoshimoto ◽  
...  
Keyword(s):  
Capillary Electrophoresis ◽  
Mammalian Cells ◽  
Dna Aptamer ◽  
Dna Aptamers ◽  
Aptamer Selection ◽  
Selection For ◽  
First Time ◽  
Selection Of

A single-round DNA aptamer selection for mammalian cells was successfully achieved for the first time using a capillary electrophoresis (CE)-based methodology.

scholarly journals Electronic origin of the dependence of hydrogen bond strengths on nearest-neighbor and next-nearest-neighbor hydrogen bonds in polyhedral water clusters (H2O)n, n = 8, 20 and 24

2016 ◽  
Vol 18 (29) ◽  
pp. 19746-19756 ◽  
Author(s):  
Suehiro Iwata ◽  
Dai Akase ◽  
Misako Aida ◽  
Sotiris S. Xantheas
Keyword(s):  
Hydrogen Bond ◽  
Hydrogen Bonds ◽  
Nearest Neighbor ◽  
Water Clusters ◽  
Hydrogen Donor ◽  
Donor And Acceptor ◽  
Bond Strengths

Comparison of the sum of the characteristic factors for some of the typical hydrogen donor and acceptor pairs with the CT term/kJ mol−1 (the upper value) and the O⋯O distance/in cubic (H2O)8.

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