Synthesis and biological properties of beta-turned Abeta(31-35) constrained analogues.
A series of constrained pentapeptide analogues of the fragment Abeta(31-35) has been prepared using solid phase synthesis protocols. The results of conformational studies and surface plasmon resonance (SPR) experiments seem to indicate that the affinity of these constrained analogues for immobilized Abeta(25-35) peptide could be related to their ability to adopt a Leu34N-Ile31O beta-turn-like folded conformation.
Pérez de Vega
M Jesús
MJ
Instituto de Química Médica (CSIC), Juan de la Cierva, 3, 28006 Madrid, Spain. pdevega@iqm.csic.es
Baeza
José Luis
JL
García-López
M Teresa
MT
Vila-Perelló
Miquel
M
Jiménez-Castells
Carmen
C
Simón
Ana María
AM
Frechilla
Diana
D
del Río
Joaquin
J
Gutiérrez-Gallego
Ricardo
R
Andreu
David
D
González-Muñiz
Rosario
R
D016229:Amyloid beta-Peptides / Q000138:chemical synthesis* / Q000737:chemistry* / Q000494:pharmacology; D000818:Animals; D015153:Blotting, Western; D002470:Cell Survival; D002478:Cells, Cultured; D006624:Hippocampus / Q000166:cytology / Q000378:metabolism; D007103:Immobilization; D015394:Molecular Structure; D009474:Neurons / Q000166:cytology / Q000378:metabolism; D017433:Protein Structure, Secondary; D051381:Rats; D017208:Rats, Wistar; D020349:Surface Plasmon Resonance
D016229:Amyloid beta-Peptides