The pyridoxal Schiff bases of the polypeptides poly(l-lysine), poly(l-ornithine), and poly(l-α,γ-diaminobutyric acid) were prepared and investigated in water/methanol by CD spectra and equilibrium dialysis experiments. Only the poly(l-α,γ-diaminobutyric acid) derivative is characterized by a relevant optical activity similar to that found in pyridoxal enzymes. The stereospecific interactions between the pyridoxylideneimine group and the polypeptide chain prevent the hydrolysis reaction of the aldimine bond.
Conformational studies on the pyridoxal Schiff bases of polypeptides / Dentini, Mariella; G., Perretti; Savino, Maria; DE SANTIS, Pasquale; A. S., Verdini. - In: BIOPOLYMERS. - ISSN 0006-3525. - STAMPA. - 17:4(1978), pp. 897-908. [10.1002/bip.1978.360170408]
Conformational studies on the pyridoxal Schiff bases of polypeptides
DENTINI, Mariella;SAVINO, Maria;DE SANTIS, Pasquale;
1978
Abstract
The pyridoxal Schiff bases of the polypeptides poly(l-lysine), poly(l-ornithine), and poly(l-α,γ-diaminobutyric acid) were prepared and investigated in water/methanol by CD spectra and equilibrium dialysis experiments. Only the poly(l-α,γ-diaminobutyric acid) derivative is characterized by a relevant optical activity similar to that found in pyridoxal enzymes. The stereospecific interactions between the pyridoxylideneimine group and the polypeptide chain prevent the hydrolysis reaction of the aldimine bond.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.