Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 142, Issue 37, Pages 15870-15875Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.0c06143
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Funding
- National Institutes of Health [GM097562]
- National Science Foundation [CHE 1808096]
- Ministry of Science and Higher Education, Republic of Poland (Mobility Plus Grant) [1647/MOB/V/2017/0]
- ALS-ENABLE program - National Institutes of Health, National Institute of General Medical Sciences [P30 GM124169-01, DE-AC02-05CH11231]
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Amyloidogenic peptides and proteins are rich sources of supramolecular assemblies. Sequences derived from well-known amyloids, including A beta, human islet amyloid polypeptide, and tau have been found to assemble as fibrils, nanosheets, ribbons, and nanotubes. The supramolecular assembly of medin, a 50-amino acid peptide that forms fibrillary deposits in aging human vasculature, has not been heavily investigated. In this work, we present an X-ray crystallographic structure of a cyclic beta-sheet peptide derived from the 19-36 region of medin that assembles to form interpenetrating cubes. The edge of each cube is composed of a single peptide, and each vertex is occupied by a divalent metal ion. This structure may be considered a metal-organic framework (MOF) containing a large peptide ligand. This work demonstrates that peptides containing Glu or Asp that are preorganized to adopt beta-hairpin structures can serve as ligands and assemble with metal ions to form MOFs.
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