Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1376838 | Bioorganic & Medicinal Chemistry Letters | 2008 | 5 Pages |
Abstract
A series of constrained pentapeptide analogues of the fragment Aβ31–35 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 Aβ25–35 peptide could be related to their ability to adopt a Leu34N-Ile31O β-turn-like folded conformation.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slide
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
M. Jesús Pérez de Vega, 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,