NEW TWIST ON AMYLOIDS
| Autor: | Carmen Drahl |
|---|---|
| Rok vydání: | 2008 |
| Předmět: | |
| Zdroj: | Chemical & Engineering News Archive. 86:7 |
| ISSN: | 2157-4936 0009-2347 |
| DOI: | 10.1021/cen-v086n013.p007 |
| Popis: | AGGREGATES OF DIFFERENT types of amyloid-forming peptides have different chiralities, a new study shows ( J. Am. Chem. Soc. , DOI: 10.1021/ja800328y). The finding gives clues about how these different peptides assemble and raises questions about the relationship between amino acid sequence, handedness, and amyloid-related ailments such as Alzheimer’s disease. Amyloids are complex protein aggregates with multiple levels of organization. Noa Rubin, Emanuel Perugia, Michal Goldschmidt, Mati Fridkin, and Lia Addadi of the Weizmann Institute of Science in Rehovot, Israel, have now used scanning electron microscopy (SEM) to learn more about one aspect of this hierarchy—amyloid chirality. The researchers examined three different amyloid fibers, each made from multiple copies of a disease-associated peptide segment from a different protein. They found that fibers made from a serum amyloid A peptide (SAA) possess a right-handed twist, and fibers from the other two peptides twist leftward. Amyloid fibers from diffe... |
| Databáze: | OpenAIRE |
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