Identification of a human brain peptidase with the specificity to generate the N-terminus of A4/β-amyloid protein from its precursor

1992 ◽  
Vol 20 (2) ◽  
pp. 206S-206S ◽  
Author(s):  
JOHN R. McDERMOTT ◽  
J ALAN BIGGINS ◽  
ALISON M GIBSO BIGGINS
1999 ◽  
Vol 79 ◽  
pp. 51
Author(s):  
Takashi Fujita ◽  
Yuji Kimura ◽  
Yoko Komeda ◽  
Kazuhiro Takuma ◽  
Toshio Matsuda ◽  
...  

1998 ◽  
Vol 336 (2) ◽  
pp. 419-427 ◽  
Author(s):  
Omar M. A. EL-AGNAF ◽  
G. Brent IRVINE ◽  
Geraldine FITZPATRICK ◽  
W. Kenneth GLASS ◽  
David J. S. GUTHRIE

In an attempt to answer the question of whether or not the so-called tachykinin-like region of the Alzheimer β-amyloid protein [Aβ(25–35)] can act as a tachykinin, the sequences Aβ(25–35), Aβ(25–35)amide and their norleucine-35 and phenylalanine-31 analogues were synthesized. These peptides were examined with ligand binding studies, electron microscopy, CD and NMR. In all cases some differences were found between the Aβ(25–35) analogue and the corresponding Phe31 peptide. In addition, in ligand displacement studies on tachykinin NK1 receptors, only the Phe31 analogue showed activity comparable to that of genuine tachykinins. We conclude that peptides based on Aβ(25–35) but with a Phe residue at position 31 do display properties typical of a tachykinin, but that peptides with Ile at this position do not.


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