4R0W

Vvtgvta, an amyloid forming segment from alpha synuclein, residues 70-76

Summary for 4R0W

• Entry DOI: 10.2210/pdb4r0w/pdb
• Related: 4r0u
• Descriptor: Alpha-synuclein (2 entities in total)
• Functional Keywords: amyloid-like protofibril, protein fibril
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P37840
• Total number of polymer chains: 1
• Total formula weight: 645.75

Authors

Ivanova, M.I.,Eisenberg, D.S.,Sawaya, M.R. (deposition date: 2014-08-01, release date: 2014-12-17, Last modification date: 2024-04-03)

Primary citation

Li, D.,Jones, E.M.,Sawaya, M.R.,Furukawa, H.,Luo, F.,Ivanova, M.,Sievers, S.A.,Wang, W.,Yaghi, O.M.,Liu, C.,Eisenberg, D.S.
Structure-based design of functional amyloid materials.
J.Am.Chem.Soc., 136:18044-18051, 2014

PubMed Abstract: Amyloid fibers, once exclusively associated with disease, are acquiring utility as a class of biological nanomaterials. Here we introduce a method that utilizes the atomic structures of amyloid peptides, to design materials with versatile applications. As a model application, we designed amyloid fibers capable of capturing carbon dioxide from flue gas, to address the global problem of excess anthropogenic carbon dioxide. By measuring dynamic separation of carbon dioxide from nitrogen, we show that fibers with designed amino acid sequences double the carbon dioxide binding capacity of the previously reported fiber formed by VQIVYK from Tau protein. In a second application, we designed fibers that facilitate retroviral gene transfer. By measuring lentiviral transduction, we show that designed fibers exceed the efficiency of polybrene, a commonly used enhancer of transduction. The same procedures can be adapted to the design of countless other amyloid materials with a variety of properties and uses.

PubMed: 25474758
DOI: 10.1021/ja509648u

Experimental method

X-RAY DIFFRACTION (1.5 Å)