Premium
Hormone‐Receptor Interactions. Synthesis and Conformational Study of cyclo ‐ L ‐Cystathionine
Author(s) -
Fauchère JeanLuc,
Muthukumaraswamy Natesa,
TunKyi Aung,
Schwyzer Robert
Publication year - 1976
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19760590631
Subject(s) - chemistry , cystine , stereochemistry , disulfide bond , cystathionine beta synthase , methylene bridge , ring (chemistry) , methylene , lanthionine , amino acid , cysteine , medicinal chemistry , organic chemistry , biochemistry , methionine , enzyme
The purpose of this work was to see whether the replacement of a sulfur atom in a cystine disulfide bridge by a methylene group is an only superficial ‘isosteric’ substitution, i.e. with regard to size, hydrophobia, bond angles, etc. , or whether it would also encompass such parameters as preferred conformations in solution ( M ‐ or P ‐helicity of the bridge). The methods involved the synthesis of a model compound, cyclo ‐ L ‐cystathionine ( cyclo ‐ L ‐carbacystine), and its investigation by 1 H‐ and 13 C‐NMR. It is concluded that the conformations of the CH 2 (β)CH 2 (γ)SCH 2 (β') bridge, and of the diketopiperazine ring are closely similar to the analogous elements in cyclo ‐ L ‐cystine (DMSO as solvent). This knowledge might help to explain the fact that carba analogs of heterodetic‐cyclic polypeptide hormones are often biologically very active.