82082-82-4Relevant academic research and scientific papers
Role of basic and acidic fragments in delicious peptides (Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala) and the taste behavior of sodium and potassium salts in acidic oligopeptides.
Nakata,Takahashi,Nakatani,Kuramitsu,Tamura,Okai
, p. 689 - 693 (2007/10/02)
The role of the acidic fragment (Asp-Glu-Glu) in delicious peptides was investigated in detail by using the Na+ or K+ salts of acidic oligopeptides so that amount of Na+ or K+ intake of peptides composed of acidic amino acids could be varied by changing their sequences. The taste of these peptides was confirmed to vary with Na+ or K+ intake. Additionally, in order to study the role of basic (Lys-Gly) and acidic (Asp-Glu-Glu) fragments in delicious peptides for producing the taste, five delicious peptide analogs, Ser-Leu-Ala-Lys-Gly-Asp-Glu-Glu, Ser-Leu-Ala-Asp-Glu-Glu-Lys-Gly, Lys-Gly-Ser-Leu-Ala-Asp-Glu-Glu, Lys-Gly-Asp-Glu-Glu, and Glu-Glu-Asp-Gly-Lys, were synthesized. The intensity of the umami and/or salty taste of these peptides and their Na salts was almost the same, despite their chemical structures being different. These results indicate that the acidic fragment as well as the basic fragment plays an important role in the taste production and intensity of delicious peptides, and that an umami or salty taste can be produced by the localization of the cation of the basic fragment and the anion of the acidic fragment.
Photoinduced Electron Transfer on a Single α-Helical Polypeptide Chain
Sisido, Masahiko,Tanaka, Ryo,Inai, Yoshihito,Imanishi, Yukio
, p. 6790 - 6796 (2007/10/02)
Electron transfer on an α-helical polypeptide carrying the sequence L-p-(dimethylamino)phenylalanine (dmaPhe)-L-alanine-L-1-pyrenylalanine (pyrAla) at the midpoint of an α-helical poly(γ-benzyl L-glutamate) chain was studied.Conformational energy calculation for the side-chain orientations predicted that only one type of orientation is allowed for both the dmaPhe and the pyrAla units.The center-to-center (edge-to-edge) distance between the two chromophores was estimated to be 13.2 (9.4) Angstroem.The fluorescence spectrum showed no exciplex emission in thepolypeptide, in contrast to the strong exciplex observed for a model tripeptide having the same dmaPhe-Ala-pyrAla sequence.The rate of electron transfer was calculated from the decay times of pyrenyl fluorescence of the polypeptide in trimethyl phosphate and in tetrahydrofuran solutions.The ket was on the order of 1E5 (s-1).The activation enthalpy was 1.4 kcal mol-1 in trimethyl phosphate and smaller than 1 kcal mol-1 in less polar solvents near room temperature.It was even smaller at lower temperatures.The activation entropy was less than -25 eu, suggesting a nonadiabatic electron transfer.In contrast to the slow electron transfer in the polypeptide, the rate constant for the model tripeptide was on the order of 1E7-1E8 (s-1) around room temperature, and the activation enthalpy was higher than that in the polypeptide case.
Variation in Bitterness Potency When Introducing Gly-Gly Residue into Bitter Peptides
Shinoda, Ichizo,Nosho, Yasuharu,Kouge, Katsushige,Ishibashi, Norio,Okai, Hideo,et al.
, p. 2103 - 2110 (2007/10/02)
We previously reported that Gly-Gly-Arg-Pro and Arg-Pro-Gly-Gly, the derivatives of a bitter peptide Arg-Pro, had no bitterness although Gly-Arg-Pro and Arg-Pro-Gly had a bitter taste at the same level as that of Arg-Pro.To elucidate the mechanism of elimination of bitterness by the introduction of the Gly-Gly residues, we synthesized Gly-Gly derivatives of other bitter peptides such as Phe-Phe, Val-Val-Val, Arg-Pro-Phe-Phe, and examined the effectiveness of Gly-Gly residues in eliminating bitterness.We suggest that, for Arg-Pro and Val-Val-Val, the Gly-Gly residue might prevent a hydrophobic group from binding to a taste receptor.
