The aromatic or aliphatic residue of native L-alpha-aminoacids is selectively included into the hydrophobic cavity of water soluble calix[4]arene receptors. The association constants values are determined by H-1 NMR titration experiments and the binding process is further elucidated by preliminary Molecular Mechanics calculations, which give results fully consistent with the NMR data. (C) 1999 Elsevier Science Ltd. All rights reserved.
The aromatic or aliphatic residue of native L-alpha-aminoacids is selectively included into the hydrophobic cavity of water soluble calix[4]arene receptors. The association constants values are determined by H-1 NMR titration experiments and the binding process is further elucidated by preliminary Molecular Mechanics calculations, which give results fully consistent with the NMR data. (C) 1999 Elsevier Science Ltd. All rights reserved.
Complexation of native L-alpha-aminoacids by water soluble calix[4]arenes
ARENA, Giuseppe;CONTINO, Annalinda;SCIOTTO, Domenico;
1999-01-01
Abstract
The aromatic or aliphatic residue of native L-alpha-aminoacids is selectively included into the hydrophobic cavity of water soluble calix[4]arene receptors. The association constants values are determined by H-1 NMR titration experiments and the binding process is further elucidated by preliminary Molecular Mechanics calculations, which give results fully consistent with the NMR data. (C) 1999 Elsevier Science Ltd. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
