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

A chemical, structural and biological study on the β‐amyloid peptide β12–28 is reported which was carried out in order to assess the feasibility using this peptide fragment as a model of the natural β‐amyloid protein. The aggregation properties of β12–28 have been investigated by pulse field‐gradien...

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Veröffentlicht in:	Journal of peptide science 2002-10, Vol.8 (10), p.578-588
Hauptverfasser:	Rabanal, Francesc, Tusell, Josep M., Sastre, Lluis, Quintero, M. Rosa, Cruz, Montse, Grillo, Dolors, Pons, Miquel, Albericio, Fernando, Serratosa, Joan, Giralt, Ernest
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amyloid beta-Peptides - chemical synthesis Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - toxicity Amyloid beta-Peptides - ultrastructure Animals Cell Survival - drug effects Chromatography, High Pressure Liquid cytotoxicity Dose-Response Relationship, Drug Kinetics Magnetic Resonance Spectroscopy Molecular Sequence Data Peptide Fragments - chemical synthesis Peptide Fragments - chemistry Peptide Fragments - toxicity Peptide Fragments - ultrastructure pulse field-gradient NMR Rats Reproducibility of Results solid phase peptide synthesis Solubility Spectroscopy, Fourier Transform Infrared Time Factors Tumor Cells, Cultured β12-28 amyloid peptide
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