Coupling of Spectrin Repeat Modules for the Assembly of Nanorods and Presentation of Protein Domains.

ABSTRACT: Modular protein engineering is a powerful approach for fabricating high-molecular-weight assemblies and biomaterials with nanoscale precision. Herein, we address the challenge of designing an extended nanoscale filamentous architecture inspired by the central rod domain of human dystrophin, which protects sarcolemma during muscle contraction and consists of spectrin repeats composed of three-helical bundles. A module of three tandem spectrin repeats was used as a rigid building block self-assembling via coiled-coil (CC) dimer-forming peptides. CC peptides were precisely integrated to maintain the spectrin α-helix continuity in an appropriate frame to form extended nanorods. An orthogonal set of customizable CC heterodimers was harnessed for modular rigid domain association, which could be

SUBMITTER: Mezgec K 

PROVIDER: S-EPMC11503911 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature