Inhibition of beta-amyloid toxicity by short peptides containing N-methyl amino acids.

Abstract

Single N-methyl amino acid-containing peptides related to the central hydrophobic region beta16-20 (Lys-Leu-Val-Phe-Phe) of the beta-amyloid protein are able to reduce the cytotoxicity of natural beta1-42 in PC12 cell cultures. N-methyl phenylalanine analogs yield statistically significant increments in cell viability (Student's t-test < 0.01%) and are nontoxic in the same assay. These promising results indicate that these peptide molecules could be a starting point for the development of potential therapeutic compounds for the treatment of Alzheimer's disease.

• Authors: M Cruz, J M Tusell, D Grillo-Bosch, F Albericio, J Serratosa, F Rabanal, E Giralt
• Journal: The journal of peptide research : official journal of the American Peptide Society (J Pept Res) Vol. 63 Issue 3 Pg. 324-8 (Mar 2004) ISSN: 1397-002X [Print] Denmark
• PMID: 15049845 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Amino Acids
• Amyloid beta-Peptides
• Formazans
• Peptides
• Tetrazolium Salts
• MTT formazan

Topics

• Alzheimer Disease (metabolism)
• Amino Acids (chemistry)
• Amyloid beta-Peptides (antagonists & inhibitors, toxicity)
• Animals
• Biological Assay
• Cell Survival
• Formazans (analysis)
• PC12 Cells
• Peptides (chemistry, pharmacology)
• Rats
• Tetrazolium Salts (analysis)