Ternary Interactions and Implications for Third Element Alloying Potency in Al–Ce-Based Alloys

The understanding of interactions between proteins, carbohydrates, and phenolic compounds is becoming increasingly important in food science, as these interactions might significantly affect the functionality of foods. So far, research has focused predominantly on protein–phenolic or carbohydrate–phenolic interactions, separately, but these components might also form other combinations. In plant-based foods, all three components are highly abundant; phenolic acids are the most important phenolic compound subclass. However, their interactions and influences are not yet fully understood. Especially in cereal products, such as bread, being a nutritional basic in human nutrition, interactions of the mentioned compounds are possible and their characterization seems to be a worthwhile target, as the functionality of each of the components might be affected. This review presents the basics of such interactions, with special emphasis on ferulic acid, as the most abundant phenolic acid in nature, and tries to illustrate the possibility of ternary interactions with regard to dough and bread properties. One of the phenomena assigned to such interactions is so-called dry-baking, which is very often observed in rye bread.

Download Full-text

The 3.2-Å resolution structure of human mTORC2

Science Advances ◽

10.1126/sciadv.abc1251 ◽

2020 ◽

Vol 6 (45) ◽

pp. eabc1251

Author(s):

Alain Scaiola ◽

Francesca Mangia ◽

Stefan Imseng ◽

Daniel Boehringer ◽

Karolin Berneiser ◽

...

Keyword(s):

Binding Sites ◽

Neurological Disorders ◽

Mammalian Target Of Rapamycin ◽

Nucleotide Binding ◽

Ternary Interactions ◽

Firm Basis ◽

Carboxyl Terminal ◽

Biochemical Analyses ◽

Specific Inhibitors ◽

Resolution Structure

The protein kinase mammalian target of rapamycin (mTOR) is the central regulator of cell growth. Aberrant mTOR signaling is linked to cancer, diabetes, and neurological disorders. mTOR exerts its functions in two distinct multiprotein complexes, mTORC1 and mTORC2. Here, we report a 3.2-Å resolution cryo-EM reconstruction of mTORC2. It reveals entangled folds of the defining Rictor and the substrate-binding SIN1 subunits, identifies the carboxyl-terminal domain of Rictor as the source of the rapamycin insensitivity of mTORC2, and resolves mechanisms for mTORC2 regulation by complex destabilization. Two previously uncharacterized small-molecule binding sites are visualized, an inositol hexakisphosphate (InsP6) pocket in mTOR and an mTORC2-specific nucleotide binding site in Rictor, which also forms a zinc finger. Structural and biochemical analyses suggest that InsP6 and nucleotide binding do not control mTORC2 activity directly but rather have roles in folding or ternary interactions. These insights provide a firm basis for studying mTORC2 signaling and for developing mTORC2-specific inhibitors.

Download Full-text

Binary versus ternary interactions in a completely miscible three-polymer blend system: Poly(?-caprolactone) with two different methacrylic polymers

Journal of Polymer Science Part B Polymer Physics ◽

10.1002/polb.10130 ◽

2002 ◽

Vol 40 (8) ◽

pp. 747-754 ◽

Cited By ~ 11

Author(s):

Su-Chiu Lee ◽

E. M. Woo

Keyword(s):

Polymer Blend ◽

Ternary Interactions ◽

Poly Caprolactone ◽

Binary Versus

Download Full-text

On the existence of ternary interactions in ion exchange

AIChE Journal ◽

10.1002/aic.690340425 ◽

1988 ◽

Vol 34 (4) ◽

pp. 702-703

Author(s):

Charles N. Haas

Keyword(s):

Ion Exchange ◽

Ternary Interactions

Download Full-text

Abstract PR2: A systems biology approach to elucidating the consequences of complex ternary interactions of heparin, FGF ligands, and FGF receptor on downstream signaling in NSCLC cells

10.1158/1538-7445.csb12-pr2 ◽

2012 ◽

Author(s):

Diana H. Chai ◽

Jaeyeon Kim ◽

Jannik Vollmer ◽

Andrijana Radivojevic ◽

Jitendra Kanodia ◽

...

Keyword(s):

Systems Biology ◽

Fgf Receptor ◽

Downstream Signaling ◽

Ternary Interactions

Download Full-text

Preliminary Studies on the Use of Reactive Distillation in the Production of Beverage Spirits

Beverages ◽

10.3390/beverages5020029 ◽

2019 ◽

Vol 5 (2) ◽

pp. 29 ◽

Cited By ~ 1

Author(s):

Jacob Rochte ◽

Kris Berglund

Keyword(s):

Gas Chromatography ◽

Butyric Acid ◽

Distillation Column ◽

Reactive Distillation ◽

Ethyl Butyrate ◽

Alcoholic Beverages ◽

Large Excess ◽

On Demand ◽

Distillation System ◽

Ternary Interactions

Distilled alcoholic beverages have been produced through fermentation and distillation for centuries but have not purposefully involved a chemical reaction to produce a flavoring. Introducing a microorganism to produce butyric acid along with the typical yeast ethanol fermentation sets up a reactive distillation system to flavor a spirit with ethyl butyrate and butyric acid. The ternary interactions of water, ethanol, and butyric acid allow all three to vaporize in the stripping distillation, thus they are concentrated in the low wines and give a large excess of ethanol compared to butyric acid for better reaction completion. The stripping distillation has also been modeled on Aspen Plus® V9 software (by Aspen Technology, Inc. Bedford, MA, USA) and coincides well with a test stripping distillation at the bench scale. Amberlyst® 15 wet catalyst was added to a subsequent distillation, resulting in the production of the desired ethyl butyrate in the distillate, measured by gas chromatography. Primary sensory evaluation has determined that this process has a profound effect on the smell of the spirit with the main flavor being similar to fruity bubble gum. The current results will provide a pathway for creating spirits with a desired flavor on demand without acquiring a heavy capital cost if a beverage distillation column is already purchased.

Download Full-text

Ternary interactions in a humic acid–Cd–bacteria system

Chemical Geology ◽

10.1016/s0009-2541(01)00305-9 ◽

2001 ◽

Vol 180 (1-4) ◽

pp. 55-65 ◽

Cited By ~ 36

Author(s):

Peter G Wightman ◽

Jeremy B Fein

Keyword(s):

Humic Acid ◽

Ternary Interactions

Download Full-text

Species-specific valid ternary interactions of HIV-1 Env-gp120, CD4, and CCR5 as revealed by an adaptive single-amino acid substitution at the V3 loop tip

Journal of Virology ◽

10.1128/jvi.02177-20 ◽

2021 ◽

Author(s):

Takaaki Koma ◽

Masaru Yokoyama ◽

Osamu Kotani ◽

Naoya Doi ◽

Nina Nakanishi ◽

...

Keyword(s):

Amino Acid ◽

Molecular Interactions ◽

Md Simulations ◽

Single Amino Acid ◽

V3 Loop ◽

Cell Tropism ◽

Binding Ability ◽

Ternary Interactions ◽

Species Specific ◽

Hiv 1

Molecular interactions of the variable envelope gp120 subunit of HIV-1 with two cellular receptors are the first step of viral infection, thereby playing pivotal roles in determining viral infectivity and cell tropism. However, the underlying regulatory mechanisms for interactions under gp120 spontaneous variations largely remain unknown. Here we show an allosteric mechanism in which a single gp120 mutation remotely controls the ternary interactions between gp120 and its receptors for the switch of viral cell tropism. Virological analyses showed that a G310R substitution at the tip of the gp120 V3 loop selectively abolished the viral replication ability in human cells, despite evoking enhancement of viral replication in macaque cells. Molecular dynamics (MD) simulations predicted that the G310R substitution at a site away from the CD4 interaction site selectively impeded the binding ability of gp120 to human CD4. Consistently, virions with the G310R substitution exhibited a reduced binding ability to human lymphocyte cells. Furthermore, the G310R substitution influenced the gp120-CCR5 interaction in a CCR5-type dependent manner as assessed by MD simulations and an infectivity assay using exogenously expressed CCR5s. Interestingly, an I198M mutation in human CCR5 restored the infectivity of the G310R virus in human cells. Finally, MD simulation predicted amino acid interplays that physically connect the V3 loop and gp120 elements for the CD4 and CCR5 interactions. Collectively, these results suggest that the V3 loop tip is a cis-allosteric regulator that remotely controls intra- and inter-molecular interactions of HIV-1 gp120 for balancing ternary interactions with CD4 and CCR5. IMPORTANCE Understanding molecular bases for viral entry into cells leads to the elucidation of one of major viral survival strategies, and thus to the development of new effective antiviral measures. As experimentally shown recently, HIV-1 is highly mutable and adaptable in growth-restrictive cells such as those of macaque origin. HIV-1 initiates its infection by sequential interactions of Env-gp120 with two cell surface receptors, CD4 and CCR5. A recent epoch-making structural study has disclosed that CD4-induced conformation of gp120 is stabilized upon binding of CCR5 to the CD4-gp120 complex, whereas its biological significance remains totally unknown. Here, from a series of mutations found in our extensive studies, we identified a single-amino acid adaptive mutation at the V3 loop tip of Env-gp120 critical for its interaction with both CD4 and CCR5 in a host cell species-specific way. This remarkable finding would certainly provoke and accelerate studies to precisely clarify the HIV-1 entry mechanism.

Download Full-text