Accessing Three-Dimensional Crystals with Incorporated Guests through Metal-Directed Coiled-Coil Peptide Assembly

Manish Nepal, Michael J. Sheedlo, Chittaranjan Das, Jean Chmielewski

Research output: Contribution to journalArticlepeer-review

36 Scopus citations

Abstract

Obtaining three-dimensional (3D) protein and peptide crystals on demand requires a precisely orchestrated hierarchical assembly of biopolymer building blocks. In this work, we disclose a metal-ion-mediated strategy to assemble trimeric coiled-coil peptides in a head-to-tail fashion into linear strands with interstrand interactions. This design led to hexagonal 3D peptide crystal formation within 30 min in the presence of divalent metal ions. The crystal morphology could be controlled by varying the metal ion/peptide ratio, resulting in hexagonal discs to rods. Diffraction studies elucidated the head-to-tail arrangement of the coiled-coil linear strands and their hexagonal, antiparallel packing within the crystal. Unsatisfied ligands at the hexagonal ends of the crystals were harnessed as a powerful means to direct His-tagged fluorophores to distinct locations within the crystals. Overall, the designed hierarchical assembly provides a facile means to obtain 3D peptide crystals and incorporate His-tag-based cargoes and may have potential use in drug delivery and sensor design.

Original languageEnglish (US)
Pages (from-to)11051-11057
Number of pages7
JournalJournal of the American Chemical Society
Volume138
Issue number34
DOIs
StatePublished - Aug 31 2016
Externally publishedYes

Bibliographical note

Funding Information:
This work was supported by the National Science Foundation through Grant CHE1609406. We thank Rashmi Shrestha for assistance with the crystallographic data and Bart Kahr for helpful discussions

Publisher Copyright:
© 2016 American Chemical Society.

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