Structure-taste relationships of some dipeptides

Mazur, Robert H.; Schlatter, James M.; Goldkamp, Arthur H.

doi:10.1021/ja01038a046

Cited by 286 publications

(108 citation statements)

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“…Consequently, in aspartame, the COOCH 3 group must be considered as only a sweetness amplifying group, increasing the sweetness potency by a factor of about 3.5 in comparison with a CH 3 group. Now if we consider the hydrophobic moieties of aspartame and alitame, it is known that the replacement in aspartame (Figure 5a) of the phenyl group by a hydrogen atom leads to a compound (Figure 5b) which is not sweet at all in man (Mazur et al, 1969). In the same way, the replacement of the 2,2,4,4-tetramethylthietanyl group of alitame (Figure 5c) by a hydrogen atom leads to an unsweet molecule ( Figure 5d) (Sukehiro et al, 1977).…”

Section: Discussionmentioning

confidence: 99%

Evolution of the Sweetness Receptor in Primates. I. Why Does Alitame Taste Sweet in all Prosimians and Simians, and Aspartame only in Old World Simians?

1995

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In the order Primates the responses to sucrose, alitame and aspartame were ascertained. All primates tested to date like sucrose and prefer this sweet substance to tap water. The artificial dipeptide aspartame was found to be not sweet in Prosimii and Platyrrhini (New World monkeys). Only the Cercopithecoidea (Old World monkeys) and Hominoidea (apes and humans) show the same response to aspartame and to sucrose. In contrast, all primates tested so far prefer alitame, another artificial dipeptide sweetener, which is structurally closely related to aspartame. This phylogenetic difference is consistent with the existence in catarrhine primates of a sweetness receptor containing two differently located hydrophobic recognition sites, one for the hydrophobic binding site of alitame, the other for the hydrophobic binding site of aspartame. On the basis of these results, it is suggested that the alitame-related hydrophobic recognition site, which is found in the sweetness receptor of all primates, could be a requisite for the interaction of the receptor with sucrose, while the aspartame-related hydrophobic recognition site, which is found exclusively in the sweetness receptor of Old World simians, could have been a crucial factor in the improvement in detection or selection of sucrose in foods, so favouring the mental development of these simians and maybe the emergence of humans.

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Section: Discussionmentioning

confidence: 99%

Evolution of the Sweetness Receptor in Primates. I. Why Does Alitame Taste Sweet in all Prosimians and Simians, and Aspartame only in Old World Simians?

1995

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“…The condensation product, Z-Phe20Me is highly insoluble in aqueous solution, and it is found almost exclusively in the organic solvent in a biphasic system, so the reaction can be analyzed as being almost irreversible. Here, we studied the thermolysin-catalyzed synthesis of N-(benzyloxycarbony1)-L-aspartyl-L-phenylalanine methyl ester (Z-Asp-PheOMe), a precursor of the synthetic sweetener aspartame [2], by condensing N-(benzyloxycarbony1)-L-aspartic acid (Z-Asp) and L-phenylalanine methyl ester (PheOMe), as a model reaction forming a soluble condensation product. The overall reaction mechanism is expressed by Eqn (1).…”

mentioning

confidence: 99%

Kinetics and equilibrium of enzymatic synthesis of peptides in aqueous/organic biphasic systems

Nakanishi

Kimura

Matsuno

1986

European Journal of Biochemistry

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We studied kinetics and the equilibrium relationship for the thermolysin-catalyzed synthesis of N-(benzyloxycarbony1)-L-aspartyl-L-phenylalanine methyl ester (Z-Asp-PheOMe) from N-(benzyloxycarbony1)-L-aspartic acid (Z-Asp) and L-phenylalanine methyl ester (PheOMe) in an aqueous-organic biphasic system. This is a model reaction giving a condensation product with dissociating groups. The kinetics for the synthesis of Z-Asp-PheOMe in aqueous solution saturated with ethyl acetate was expressed by a rate equation for the rapid-equilibrium random bireactant mechanism, and the reverse hydrolysis reaction was zero-order with respect to Z-Asp-PheOMe concentration. The courses of synthesis of Z-Asp-PheOMe in the biphasic system were well explained, by the rate equations obtained for the aqueous solution and by the partition of substrate and condensation product between the both phases. The rate of synthesis in the biphasic system was much lower than in aqueous solution due to the unfavorable partition of PheOMe in the aqueous phase.The equation for the equilibrium yield of Z-Asp-PheOMe in the biphasic system was derived assuming that only the non-ionized forms of the substrate and condensation product exist in the organic phase. It was found theoretically and experimentally that the yield of Z-Asp-PheOMe is maximum at the aqueous-phase pH of around 5, lower than for synthesis in aqueous solution. The effect of the organic solvent on the rate and equilibrium for the synthesis of Z-Asp-PheOMe could be explained by the variation in the partition coefficient.The effect of the partitioning of substrate on the aqueous-phase pH change was also shown.The kmetics of the thermolysin-catalyzed synthesis of N-(benzyloxycarbonyl)-L-phenylalanyl-L-phenylalanine methyl ester (Z-PhezOMe) in an aqueous/organic biphasic system has been discussed in the preceding paper [l]. The condensation product, Z-Phe20Me is highly insoluble in aqueous solution, and it is found almost exclusively in the organic solvent in a biphasic system, so the reaction can be analyzed as being almost irreversible. Here, we studied the thermolysin-catalyzed synthesis of N-(benzyloxycarbony1)-L-aspartyl-L-phenylalanine methyl ester (Z-Asp-PheOMe), a precursor of the synthetic sweetener aspartame [2], by condensing N-(benzyloxycarbony1)-L-aspartic acid (Z-Asp) and L-phenylalanine methyl ester (PheOMe), as a model reaction forming a soluble condensation product. The overall reaction mechanism is expressed by Eqn (1).Z-Asp-PheOMe is more soluble (about 40 mM at 40°C and pH 6) than Z-PhezOMe (about 5 pM at 40°C and pH 7) be- cause of its side carboxylic acid. The purpose of this study was to elucidate theoretically and experimentally the equilibrium yield of the reaction as well as the rate of the synthesis of Z-Asp-PheOMe in an aqueous/organic biphasic system. Various factors affecting the equilibrium yield and reaction rate, such as the aqueous-phase pH, the volume ratio of the organic to aqueous phases, and the organic solvent, were examined quantitatively.

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“…To this end we introduced an ethylene bridge between the of the N i , from the reversed peptide bond (C i O-N iϩ1 H3 N i H-C iϩ1 O), and the original N iϩ3 forming a [1,4,7]triazecane-3,8,10-trione ring system that replaces the C i O ⅐ ⅐ ⅐ HN iϩ3 10-membered hydrogenbonded ring of a classical ␤-turn ( Figure 13). 68 The novel N i -to-N iϩ3 -ethylene-bridged partially modified RI tetrapeptide ␤-turn mimetic (EBRIT-BTM) was synthesized efficiently from the fully protected N,NЈ- …”

Section: Variations On the Themementioning

confidence: 99%

The partial retro–inverso modification: A road traveled together

Chorev

2005

Biopolymers

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Structure-taste relationships of some dipeptides

Cited by 286 publications

References 0 publications

Evolution of the Sweetness Receptor in Primates. I. Why Does Alitame Taste Sweet in all Prosimians and Simians, and Aspartame only in Old World Simians?

Evolution of the Sweetness Receptor in Primates. I. Why Does Alitame Taste Sweet in all Prosimians and Simians, and Aspartame only in Old World Simians?

Kinetics and equilibrium of enzymatic synthesis of peptides in aqueous/organic biphasic systems

The partial retro–inverso modification: A road traveled together

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