A novel amyloid designable scaffold and potential inhibitor inspired by GAIIG of amyloid beta and the HIV-1 V3 loop
| Autor: | Sai Vamshi R. Jonnalagadda, Chrysoula Kokotidou, Matthew W. Bowler, Phanourios Tamamis, Mark J. van Raaij, Estelle Mossou, Apostolos Chatzoudis, V. Trevor Forsyth, Chrysanthi Pinelopi Apostolidou, Mateo Seoane-Blanco, Antonio L. Llamas-Saiz, Marianna Kotzabasaki, Joseph M. Jakubowski, Anna Mitraki, Edward P. Mitchell, Asuka A. Orr |
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| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Scaffold Amyloid Amyloid beta Biophysics Human immunodeficiency virus (HIV) Sequence (biology) Peptide HIV Envelope Protein gp120 V3 loop Crystallography X-Ray medicine.disease_cause Biochemistry Protein Structure Secondary 03 medical and health sciences Structural Biology mental disorders Genetics medicine Humans Molecular Biology chemistry.chemical_classification Amyloid beta-Peptides biology Cell Biology Amyloid fibril 030104 developmental biology chemistry HIV-1 biology.protein |
| Zdroj: | 'FEBS Letters ', vol: 592, pages: 1777-1788 (2018) |
| Popis: | The GAIIG sequence, common to the amyloid beta peptide (residues 29-33) and to the HIV-1 gp120 (residues 24-28 in a typical V3 loop), self-assembles into amyloid fibrils, as suggested by theory and the experiments presented here. The longer YATGAIIGNII sequence from the V3 loop also self-assembles into amyloid fibrils, of which the first three and the last two residues are outside the amyloid GAIIG core. We postulate that this sequence, with suitably selected modifications at the flexible positions, can serve as a designable scaffold for novel amyloid-based materials. Moreover, we report the single crystal X-ray structure of the beta-breaker peptide GAIPIG at 1.05 Å resolution. The structural information provided in this study could serve as the basis for structure-based design of potential inhibitors of amyloid formation. |
| Databáze: | OpenAIRE |
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