Structural, kinetic and cytotoxicity aspects of 12–28 β-amyloid protein fragment: a reappraisal

✍ Scribed by Francesc Rabanal; Josep M. Tusell; Lluis Sastre; M. Rosa Quintero; Montse Cruz; Dolors Grillo; Miquel Pons; Fernando Albericio; Joan Serratosa; Ernest Giralt

• Publisher: John Wiley and Sons
• Year: 2002
• Tongue: English
• Weight: 188 KB
• Volume: 8
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.418

✦ Synopsis

A chemical, structural and biological study on the beta-amyloid peptide beta12-28 is reported which was carried out in order to assess the feasibility using this peptide fragment as a model of the natural beta-amyloid protein. The aggregation properties of beta12-28 have been investigated by pulse field-gradient NMR spectroscopy, Fourier transform infrared spectroscopy and transmission electron microscopy. The results obtained suggest that beta12-28 behaviour is comparable to that of the natural beta-amyloid protein although kinetically slower. Translational diffusion coefficients obtained by NMR on an aged beta12-28 solution suggest that the soluble peptide fraction is composed of oligomeric intermediates adopting an extended ellipsoidal assembly rather than a spherical one. The beta12-28 peptide proved to be cytotoxic in PC12 cell cultures as monitored by the MTT assay, although a lack of reproducibility was observed in the dose-response experiments.