- Chemo-enzymatic synthesis of optically active amino acids and peptides
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The industrial alkaline protease, alcalase, is stable and active in a high concentration of organic solvents and useful as a biocatalyst for (i) diastereoselective hydrolysis of peptide esters and preparation of racemization-free peptides; (ii) selective incorporation of esters of D-amino acid into peptides in t-butanol via a selective hydrolysis of esters of D,L-amino acid, followed by using the unhydrolyzed D-esters as a nucleophile in a kinetically controlled peptide bond formation; (iii) resolution of esters of amino acid in 95% t-butanol/5% water, followed by saponification of the unreacted esters to offer both enantiomers with high yield and optical purity; (iv) completely resolve amino-acid esters with high yield and optical purity via in situ racemization of the unreacted antipode catalyzed by pyridoxal 5-phosphate; (v) cryobioorganic synthesis of peptides with increased yields 15%-40% of peptide bond formation by reaction at 5 °C instead of 25-30 °C of a kinetically controlled enzymatic reaction in alcohols.
- Chen, Shui-Tein,Wang, Kung-Tsung
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p. 301 - 311
(2007/10/03)
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- Chemo-enzymatic synthesis of Fmoc-peptide fragments
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Optically pure Fmoc-peptide fragments have been prepared via dicyclohexylcarbodiimide coupling of N-protected amino acids with amino cid esters, followed by enzyme-catalyzed ester hydrolysis by alcalase with a high concentration of organic solvent in a hi
- Chen,Hsiao,Chang,Wang
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p. 391 - 398
(2007/10/02)
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- Facile Synthesis of N-Protected Peptide Fragments using Polymer-Bound 1-Hydroxybenzotriazole as an Active Ester
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Using polystyrene-bound 1-hydroxybenzotriazole as an active ester and an amino acid or peptide, temporarily C-terminal-protected by a phase-transfer reagent, as a nucleophile, C-terminal-free peptide fragments can be synthesized with very high yield and p
- Chen, Shui-Tein,Chang, Chung-Ho,Wang, Kung-Tsung
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p. 1967 - 1975
(2007/10/02)
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