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Snake venom peptides

A. L. Harvey, Snake Venom Peptides. In Handbook of BioiogicaiiyActive Peptides] J. Kastin, Ed. Elsevier Amsterdam, 2006 p 355. [Pg.299]

The first important AGE inhibitors were snake venom peptides. Their isolations and characterizations have been described in comprehensive reviews by Ferreira (70, 71) and by Cushman and Ondetti (72-74). [Pg.20]

Important Snake Venom Peptide Inhibitors of Angiotensin-Converting Enzyme... [Pg.21]

In agreement with the enzyme s specificity, acidic amino acids and N-alkylated amino acids afforded poor inhibitors. The discovery that lysine in the penultimate position provided good inhibition was at the time unprecedented in the ACE substrate or snake venom peptide literature, and this development was pursued with additional analogues (Table VI). Excellent activity was obtained with arginine and with higher and lower homologues of lysine. Even the s-N-acetyllysine analogue 33 (Table VI) was active. [Pg.31]

Peptide sequences related to those of snake venom peptides had already been used to define the structural requirements for peptide inhibitors of angiotensin-converting enzyme. Peptides are unstable in vivo and poorly ab-... [Pg.432]

The snake venom peptide BPPsa and captopril bind at the active site of ACE in a competitive manner, thereby-replacing angiotensin I and bradykinin. [Pg.219]


See other pages where Snake venom peptides is mentioned: [Pg.379]    [Pg.291]    [Pg.21]    [Pg.23]    [Pg.24]    [Pg.1472]    [Pg.1474]    [Pg.14]    [Pg.166]    [Pg.34]    [Pg.6]    [Pg.394]    [Pg.1119]    [Pg.52]    [Pg.14]   
See also in sourсe #XX -- [ Pg.2 , Pg.6 , Pg.881 ]

See also in sourсe #XX -- [ Pg.6 ]




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