What question did this study set out to answer?

To explore the mechanical properties of fibers made from immunoglobulin domains derived from muscle proteins.

February 8, 2026Advanced Functional Materials0 citations

Muscle‐Inspired Fibers from Immunoglobulin Domains Combine Superior Mechanical Performance, Energy Damping, and Shape Memory Properties

SSShri Venkatesh Subramani QGQingyue Guo HGHuamin Gao

Puntos clave

To explore the mechanical properties of fibers made from immunoglobulin domains derived from muscle proteins.
Fabricated fibers from microbially-synthesized immunoglobulin domains.
Tested mechanical properties including tensile strength and energy damping.
Assessed shape recovery and stability under humid conditions.
Filamin-derived immunoglobulin fibers achieved tensile strength of 412 MPa.
High toughness of 120 MJ/m³ and 89% mechanical stability under 90% humidity observed.
Fibers showed 80% energy damping and nearly complete shape recovery over multiple cycles.

Resumen

ABSTRACT Animal muscle is an intriguing natural material whose mechanical properties arise from sequence‐diverse protein domains, many of which remain unexplored for material design. Among them, Immunoglobulin‐like (Ig) domains act as molecular springs that can unfold and refold repetitively without losing function, dissipating mechanical energy as heat, making them promising building blocks for next‐generation protein‐based materials (PBMs). In this study, we translate these molecular features to the macroscale by fabricating fibers from microbially‐synthesized Ig domains of various muscle proteins. Among them, Filamin‐derived Ig fibers ( M W = 123 kDa) exhibited a unique combination of high tensile strength (412 ± 22 MPa), high toughness (120 ± 17 MJ/m 3 ), remarkable mechanical stability (∼89%) under 90% humidity, high energy damping capacity (∼80%), and complete shape recovery (∼100%) over repeated loading–unloading cycles. Our results further revealed molecular mechanisms underlying these properties: (i) Ig domain hydrophobicity strongly correlates with fiber assembly and tensile strength, (ii) reversible unfolding–refolding of Ig domains enables efficient energy dissipation and self‐recovery, and (iii) hydrogen‐bonding networks within the amorphous matrix regulate humidity‐induced weakening. Together, these findings establish Ig domains as a new class of PBMs combining advantageous mechanical and physical properties, offering a versatile platform for developing advanced materials with tunable performance.

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