| Autor: |
Eichinger, Andreas, Rauth, Sabine, Hinz, Dominik, Feuerbach, Anna, Skerra, Arne |
| Předmět: |
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| Zdroj: |
Biological Chemistry; Apr2022, Vol. 403 Issue 5/6, p557-571, 15p |
| Abstrakt: |
Keywords: A-beta peptide; anticalin; neurodegeneration; protein engineering; X-ray structure EN A-beta peptide anticalin neurodegeneration protein engineering X-ray structure 557 571 15 04/12/22 20220401 NES 220401 Introduction Alzheimer's disease (AD) is the most prevalent form of dementia, with 10% of the human population older than 65 and even 40% older than 85 years affected ([29]). To understand the mechanisms of molecular recognition of A I i peptides by the anticalins and to gain insight into their potential as biopharmaceutical drug candidates of a novel class, we have performed crystallographic analyses of the anticalin proteins H1GA and US7 in complex with the minimal epitope peptide as well as with the full length A I i SB 40 sb target. Now, a set of 12 peptide sequences occurring in those relevant human plasma proteins and having similarity to the linear epitope SP 18 sp VFFAED SP 23 sp recognized by H1GA were synthesized with varying lengths, as octamer, dodecamer and hexadecamer peptides, on the membrane along with the target peptide, A I i SB 16-23 sb (Figure 6). Structural basis of Alzheimer -amyloid peptide recognition by engineered lipocalin proteins with aggregation-blocking activity. [Extracted from the article] |
| Databáze: |
Complementary Index |
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