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The role of membrane-promoted multi-point hydrophobic interactions between peptide catalysts and enantiomeric substrates in highly stereoselective hydrolyses of amino acid esters

✍ Scribed by Katsutoshi Ohkubo; Kenji Urabe; Junji Yamamoto; Satoshi Usui; Takashi Sagawa

Publisher: Elsevier Science
Year: 1996
Tongue: English
Weight: 296 KB
Volume: 110
Category: Article
ISSN: 1381-1169
DOI: 10.1016/1381-1169(96)00157-4

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✦ Synopsis

The 500 MHz 'H NMR NOESY spectra of membrane-promoted multi-point hydrophobic interactions between peptide catalysts and enantiomeric amino acid esters were detected for clarifying the role of muti-point interactions between the reactants in the highly stereoselective hydrolysis reactions in a vesicular membrane.

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The role of the membrane-assisted hydrophobic interaction between di-, tri-, or tetrapeptide catalysts and amino acid esters for the enhancement of stereoselective hydrolysis reactions

✍ Katsutoshi Ohkubo; Kenji Urabe; Satoshi Usui; Takashi Sagawa 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 365 KB

## Abstract The peptide catalyst having the amino acid sequence (Z‐L‐Leu (or Phe)‐L‐His) was found to be the most stereoselective among the L‐histidyl group‐containing di‐, tri‐, or tetrapeptide catalysts in the hydrolysis of enantiomeric amino acid substrates in vesicular membranes. The role of th