Structural highlights
Publication Abstract from PubMed
Amyloidogenic peptides and proteins are rich sources of supramolecular assemblies. Sequences derived from well-known amyloids, including Abeta, 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.
Interpenetrating Cubes in the X-ray Crystallographic Structure of a Peptide Derived from Medin19-36.,Howitz WJ, Wierzbicki M, Cabanela RW, Saliba C, Motavalli A, Tran N, Nowick JS J Am Chem Soc. 2020 Sep 3. doi: 10.1021/jacs.0c06143. PMID:32816461[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Howitz WJ, Wierzbicki M, Cabanela RW, Saliba C, Motavalli A, Tran N, Nowick JS. Interpenetrating Cubes in the X-ray Crystallographic Structure of a Peptide Derived from Medin19-36. J Am Chem Soc. 2020 Sep 3. doi: 10.1021/jacs.0c06143. PMID:32816461 doi:http://dx.doi.org/10.1021/jacs.0c06143
