scholarly journals Photocyclization of .GAMMA.-Chlorotiglyl-L-tryptophan Methyl Ester Yields Azocinoindole and Azepinoindole Derivatives.

1993 ◽  
Vol 41 (2) ◽  
pp. 369-372 ◽  
Author(s):  
Ryuji NAGATA ◽  
Yasuyuki ENDO ◽  
Koichi SHUDO
Keyword(s):  
Methyl Ester ◽  
Tryptophan Methyl Ester

scholarly journals Cyclisations of Tryptophans. I. Trifluoroacetylation of Nb-Methoxycarbonyl-L-tryptophan Methyl Ester in Trifluoroacetic Acid.

1994 ◽  
Vol 48 ◽  
pp. 91-93 ◽  
Author(s):  
Uffe Anthoni ◽  
Carsten Christophersen ◽  
Per Halfdan Nielsen ◽  
Erik Jonas Pedersen ◽  
Lee-Chiang Lo ◽  
...  
Keyword(s):  
Methyl Ester ◽  
Trifluoroacetic Acid ◽  
Tryptophan Methyl Ester

scholarly journals Cyclisations of Tryptophans. II. Protonated Species Derived from L-Tryptophan Methyl Ester and its Nb-Acetyl Derivative.

1995 ◽  
Vol 49 ◽  
pp. 441-445 ◽  
Author(s):  
Uffe Anthoni ◽  
Lone Chortsen ◽  
Carsten Christophersen ◽  
Per Halfdan Nielsen ◽  
David J. Timmerman-Vaughan ◽  
...  
Keyword(s):  
Methyl Ester ◽  
Acetyl Derivative ◽  
Protonated Species ◽  
Tryptophan Methyl Ester

scholarly journals Comparative studies of the specificities of α-chymotrypsin and subtilisin BPN′. Studies with flexible substrates

1972 ◽  
Vol 126 (3) ◽  
pp. 645-657 ◽  
Author(s):  
T. N. Pattabiraman ◽  
W. B. Lawson
Keyword(s):  
Methyl Ester ◽  
Binding Site ◽  
Comparative Studies ◽  
Detrimental Effect ◽  
Flexible Substrates ◽  
Enhancing Effect ◽  
Wide Range ◽  
Phenylalanine Methyl Ester ◽  
Hydrolysis Of ◽  
Tryptophan Methyl Ester

A series of arylalkanoate esters and α-acetamidoarylalkanoate esters were tested as substrates for α-chymotrypsin and subtilisin BPN′. Chymotrypsin hydrolysed N-acetyl-l-phenylalanine methyl ester and methyl 4-phenylbutyrate faster than their respective higher and lower homologues, whereas methyl 2-acetamido-6-phenylhexanoate and methyl 6-phenylhexanoate were better substrates for subtilisin than their lower homologues. N-Acetyl-l-tryptophan methyl ester and its analogue, N-acetyl-3-(1-naphthyl)-alanine methyl ester, were hydrolysed 23 times faster by chymotrypsin than by subtilisin. These results indicate that the binding site of α-chymotrypsin is roughly 1.1nm (11Å) long and curved, whereas that of subtilisin is a longer system and less curved. The stereo-specificity during the hydrolysis of typical substrates by both enzymes was found to vary over a wide range. The enhancing effect of the α-acetamido group in the l-series of substrates and the detrimental effect in the d-series of substrates also varies considerably.

scholarly journals Recognizing Amino Acid Chirality with Surface-Imprinted Polymers Prepared in W/O Emulsions

2013 ◽  
Vol 2013 ◽  
pp. 1-5 ◽  
Author(s):  
Min Jae Shin ◽  
Young Jae Shin ◽  
Seung Won Hwang ◽  
Jae Sup Shin
Keyword(s):  
Methyl Ester ◽  
Crosslinking Agent ◽  
Water Soluble ◽  
Solid Polymer ◽  
Cavity Surface ◽  
Molecularly Imprinted ◽  
Imprinted Polymers ◽  
Phenylalanine Methyl Ester ◽  
Tryptophan Methyl Ester ◽  
Enantiomeric Selectivity

A molecularly imprinted polymer was prepared by a surface molecular imprinting technique in water-in-oil (W/O) emulsion. In this technique, the solid polymer, which is molecularly imprinted at the internal cavity surface, is prepared by polymerizing W/O emulsions consisting of a water-soluble imprinted molecule, a functional host molecule, an emulsion stabilizer, and a crosslinking agent. Dioleoyl phosphate was used as an emulsion stabilizer, and this compound also acted as a monomer and a host functional group in the imprinted cavity. Divinylbenzene was used as a crosslinker. Tryptophan methyl ester and phenylalanine methyl ester were used as the target template materials. These imprinted polymers exhibited enantiomeric selectivity in absorption experiments, and the maximum separation factor was 1.58. The enantiomeric selectivity with tryptophan methyl ester was higher than that with phenylalanine methyl ester.

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