Synthesis and biological properties of beta-turned Abeta(31-35) constrained analogues

  • Bioorg Med Chem Lett. 2008 Mar 15;18(6):2078-82. doi: 10.1016/j.bmcl.2008.01.092.
M Jesús Pérez de Vega  1 ,  José Luis Baeza ,  M Teresa García-López ,  Miquel Vila-Perelló ,  Carmen Jiménez-Castells ,  Ana María Simón ,  Diana Frechilla ,  Joaquin del Río ,  Ricardo Gutiérrez-Gallego ,  David Andreu ,  Rosario González-Muñiz
Affiliations
  • 1. Instituto de Química Médica (CSIC), Juan de la Cierva, 3, 28006 Madrid, Spain. [email protected]
PMID: 18262786 DOI: 10.1016/j.bmcl.2008.01.092
Abstract

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.

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