Transglutaminase-mediated amine incorporation into substance P protects the peptide against proteolysis in vitro.
The in vitro metabolism of transglutaminase-synthesized substance P analogs has been characterized comparing their stability to that of the parent peptide. The major metabolites have been purified and their structures elucidated by mass spectrometry. Our results demonstrated that gln5 spermidine and spermine analogs of substance P possess an enhanced resistance to the action of proteases. Moreover spermine, a large size hydrophilic compound, specifically prevented the hydrolysis at Phe7-Phe8 bond.
Esposito
C
C
Department of Biochemistry and Biophysics, 2nd University of Naples, Italy. carlaesp@unina.it
Costa
C
C
Amoresano
A
A
Mariniello
L
L
Sommella
M G
MG
Caputo
I
I
Porta
R
R
D000588:Amines / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000378:metabolism; D006868:Hydrolysis; D008969:Molecular Sequence Data; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D051381:Rats; D013373:Substance P / Q000031:analogs & derivatives / Q000378:metabolism*; D011503:Transglutaminases / Q000378:metabolism*
D000588:Amines; D013373:Substance P; D011503:Transglutaminases; D007703:Peptidyl-Dipeptidase A