Optical resolution of DL-proline by forming a new diastereoisomeric solid complex with L-tartaric acid.

Yamada, Shigeki; Hongo, Chikara; Chibata, Ichiro

doi:10.1271/bbb1961.41.2413

Cited by 11 publications

(6 citation statements)

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“…A rapid and efficient method for separating the optical isomers of D,L-dmP was developed here, based on a method that proved suitable to resolve the enantiomers of D,L-Pro. 37 This method is based on the differential solubility of the complexes formed between the optical isomers of dmP and D-tartaric acid. The D,L-dmP (1.0 g/7.0 mmol, equivalent to 3.5 mmol of the L form) was dissolved in 2.0 mL of water containing 1.05 g/7.0 mmol of D-tartaric acid at room temperature.…”

Section: Methodsmentioning

confidence: 99%

“…As far as we are aware, optically pure l -dmP has not been prepared previously. A rapid and efficient method for separating the optical isomers of d , l -dmP was developed here, based on a method that proved suitable to resolve the enantiomers of d , l -Pro . This method is based on the differential solubility of the complexes formed between the optical isomers of dmP and d -tartaric acid.…”

Section: Methodsmentioning

confidence: 99%

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Retention of the Cis Proline Conformation in Tripeptide Fragments of Bovine Pancreatic Ribonuclease A Containing a Non-natural Proline Analogue, 5,5-Dimethylproline

et al. 1999

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Attention is focused on L-5,5-dimethylproline (dmP) as a substitute to lock L-proline (Pro) in a cis conformation in peptides and proteins, to prevent cis/trans isomerization when a protein with cis X-Pro peptide groups unfolds. Procedures have been developed to obtain optically pure L-dmP and to incorporate this sterically hindered residue as the central one in tripeptides that are suitable for fragment coupling to prepare synthetic proteins. Based on the sequences of residues 92-94 (Tyr-Pro-Asn:YPN) and 113-115 (Asn-Pro-Tyr: NPY) in bovine pancreatic ribonuclease A (RNase A), in which the X-Pro peptide groups are in the cis conformation, the tripeptides Ac-Tyr-dmP-Asn (YdmPN) and Ac-Asn-dmP-Tyr (NdmPY) were synthesized, and their structures were determined by 2D 1 H nuclear magnetic resonance (NMR) spectroscopy. YdmPN was found to exist solely in the cis conformation between 6 and 60 °C, whereas NdmPY was found to have some trans component that increased from about 10% to about 21% as the temperature increased over the range between 6 and 80 °C. Both YdmPN and cis-NdmPY adopt a type VI reverse turn, as does proline. The NMR structures of YdmPN and cis-NdmPY are comparable with the X-ray structures of the corresponding portions of RNase A, and the NMR structure of trans-NdmPY is compatible with the X-ray structure of the isolated tripeptide, Ac-NPY. These results demonstrate that L-dmP is a promising substitute for proline in a variety of protein problems to constrain the X-Pro peptide group to the cis conformation.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Retention of the Cis Proline Conformation in Tripeptide Fragments of Bovine Pancreatic Ribonuclease A Containing a Non-natural Proline Analogue, 5,5-Dimethylproline

et al. 1999

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“…Resolution of dh-[2-2H]Proline. DL-[2-3H]proline was resolved by a modification of the methods of Yamada et al (1977). To a stirred solution of dl-[2-3H]proline (0.4 g) and L-tartaric acid (0.26 g) in water (350 µ ) was added dropwise absolute ethanol (~3 mL) until a permanent turbidity appeared.…”

Section: Methodsmentioning

confidence: 99%

“…L-Proline (185 mg) and L-tartaric acid (125 mg) were dissolved in water (160 µ ), and the solution was left at room temperature for 30 min. The solid complex was isolated by filtration and dried in air: yield 76 mg; mp 152-154 °C [Yamada et al (1977) give 153-154 °C], The complex between D-proline and Dtartaric acid was prepared analogously.…”

Section: Methodsmentioning

confidence: 99%

Energetics of proline racemase: transition-state fractionation factors for the two protons involved in the catalytic steps

Fisher¹,

Belasco²,

Bruice³

et al. 1986

Biochemistry

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The isotope effects for the interconversion of L-proline and D-proline, catalyzed by proline racemase, have been determined in the saturated region with both [2-2H]proline and [2-3H]proline. The deuterium fractionation factors for each of the protons in flight have been obtained from two kinds of experiment: by measuring the rate of racemization of one [2-2H]proline enantiomer as it racemizes into an equilibrated pool of unlabeled proline and by measuring the deuterium content of a proline sample at the optical rotation maximum that occurs when an equimolar mixture of one deuterium-labeled enantiomer and the other unlabeled enantiomer runs to equilibrium. The tritium fractionation factors for each of the protons in flight have been determined from measurements of the rate of loss of tritium to the solvent as one [2-3H]proline enantiomer runs to equilibrium. Good agreement is found among the fractionation factors determined by each method. The deuterium fractionation factors for the two protons are not identical: that for the proton derived from L-proline is 0.375 and that for the proton derived from D-proline is 0.44. This difference has been confirmed by a double-competition experiment in which the optical rotation of a mixture of DL-[2-2H]proline and unlabeled DL-proline is followed with time. The rotation (initially zero) passes through a maximum, from which the ratio of the two fractionation factors (0.86) is obtained. These data, coupled with the equilibrium fractionation factor for the 2-position of proline (which has been determined to be 1.17), provide the transition-state factors for each of the in-flight protons, and delineate the nature of the transition state(s) for the enzyme-catalyzed racemization.

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“…Amino acids could take part in the ECL reactions with Ru(bpy) 3 2+ , which would act as oxidative-reduction coreactants of Ru(bpy) 3 2+ . The ECL mechanism of reaction between Ru(bpy) 3 2+ and proline has been discussed: at the electrode surface, the immobilized Ru(bpy) 3 2+ was oxidized to Ru(bpy) 3 3+ in eqn (1), while the negatively charged proline (pH 8.5, isoelectric point is 6.3) 40,41 was also oxidized to produce free radical in eqn. (2).…”

Section: The Discussion Of the Reaction Mechanismmentioning

confidence: 99%

A novel chiral electrochemiluminescence sensor that can discriminate proline enantiomers

Wang

Xia

et al. 2015

RSC Adv.

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Optical resolution of DL-proline by forming a new diastereoisomeric solid complex with L-tartaric acid.

Cited by 11 publications

References 0 publications

Retention of the Cis Proline Conformation in Tripeptide Fragments of Bovine Pancreatic Ribonuclease A Containing a Non-natural Proline Analogue, 5,5-Dimethylproline

Retention of the Cis Proline Conformation in Tripeptide Fragments of Bovine Pancreatic Ribonuclease A Containing a Non-natural Proline Analogue, 5,5-Dimethylproline

Energetics of proline racemase: transition-state fractionation factors for the two protons involved in the catalytic steps

A novel chiral electrochemiluminescence sensor that can discriminate proline enantiomers

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