Preparation of L- and D-3-phenyllactic acids and some of their derivatives

Shchukina, L. A.; Gromova, G. F.; Ravdel, G. A.

doi:10.1007/bf00846110

Cited by 3 publications

(3 citation statements)

References 8 publications

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“…The optical resolution of racemic 2-ethynyl-2-phenylglycolic acid using (1S,2S)-ANP was previously reported by Issei [11]. DL-Phenyllactic acid was later resolved using (1S,2S)-ANP to give diastereoisomeric salts, and then acidified with HCl to give free L-phenyllactic acid [12].…”

Section: Applications In Resolution Of Other Acidsmentioning

confidence: 99%

An Overview of Highly Optically Pure Chloramphenicol Bases: Applications and Modifications

Yang

Fang²,

Gong³

et al. 2009

MRMC

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Section: Applications In Resolution Of Other Acidsmentioning

confidence: 99%

An Overview of Highly Optically Pure Chloramphenicol Bases: Applications and Modifications

Yang

Fang²,

Gong³

et al. 2009

MRMC

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“…N-Boc-N-methyl-L-leucine 16 was coupled with -lactam benzyl ester 51 (71%), and the benzyl group was removed (∼100%) to give -lactam free acid 52. Coupling this product with benzyl 3-phenyl-Dlactate 4 18 gave the tetradepsipeptide (42%) along with a lesser amount of diastereomer, which was easily removed by chromatography. Removal of the Boc group (91%) gave tetradepsipeptide free amine 53.…”

Section: Chemistrymentioning

confidence: 99%

Restricted Conformation Analogues of an Anthelmintic Cyclodepsipeptide

Dutton¹,

Lee²,

Johnson³

et al. 2003

J. Med. Chem.

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Six analogues of the anthelmintic cyclodepsipeptide PF1022A were prepared, each containing a small ring fused to the macrocycle to restrict the number of conformations the larger ring can adopt. It was anticipated that such conformational changes could lead to enhanced biological activity and selectivity. The analogues form two series of three members each. In one series, a carbon-based molecular bridge joins the methyl of a leucine residue with the methyl of its closest lactic acid residue to form five-, six-, and seven-membered lactam rings. In the second series, a leucine residue is replaced with five-, six-, and seven-membered nitrogen heterocycles. Decreasing the size of the small ring in the lactam series increasingly distorts the macrocycle and consistently decreases activity relative to PF1022A. In the leucine series, a similar trend is observed. Molecular modeling of PF1022A along with the analogues described herein suggests that the ability to exist in a highly symmetrical conformational state is a necessary condition for biological activity.

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“…?-21.50 (c 2 in water). Shchukina, Gromova & Ravdel (1966), who prepared the compound by resolution of DL-,-phenyl-lactic acid, give Orekhovich & Sklyankina (1964) reported the synthesis of N-acetyl-L-phenylalanyl-L-.f-phenyl-lactic acid by the direct coupling of N-acetyl-L-phenylalanine and L-.f-phenyl-lactic acid by using a 'mixed-anhydride' method, and obtained a prodtict of m.p. 168-170°.…”

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confidence: 99%

The pH-dependence of the binding of competitive inhibitors to pepsin

Knowles

Sharp

Greenwell

1969

Biochemical Journal

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1. The pH-dependence of the binding to pepsin of four dipeptide competitive inhibitors is reported. Values of K(i) obtained from equilibrium-dialysis experiments agree closely with those from kinetic measurements. 2. The binding of uncharged N-acyl-dipeptide amides to pepsin is essentially independent of pH from 0.2 to 5.8. Values of K(i) for the corresponding N-acyl-dipeptide acids rise rapidly above pH3.5, and depend on the ionization of a group of apparent pK(a) 3.6. 3. The data indicate that pepsin does not undergo any gross conformation change (at least none that affects binding) over the whole pH range of its catalytic activity. The pH-dependence of the dipeptide acid inhibitors indicates that the acid anions do not bind to pepsin, presumably because of electrostatic repulsion between the inhibitor anion and a negative centre at or near the active site of the enzyme. 4. The binding of all four stereoisomers of N-acetylphenylalanylphenylalanine, of the depside analogues of the l-l- and d-l-compounds and of N-acetylglycyl-l-phenylalanine and N-acetyl-l-phenylalanylglycine was studied at pH2.2. 5. These results throw further light on the binding specificity of pepsin and on the charge nature of the active site of this enzyme.

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Preparation of L- and D-3-phenyllactic acids and some of their derivatives

Cited by 3 publications

References 8 publications

An Overview of Highly Optically Pure Chloramphenicol Bases: Applications and Modifications

An Overview of Highly Optically Pure Chloramphenicol Bases: Applications and Modifications

Restricted Conformation Analogues of an Anthelmintic Cyclodepsipeptide

The pH-dependence of the binding of competitive inhibitors to pepsin

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