Exploring Native and Designed Elastins as Protein-Based Elastocaloric Materials: A First Investigation

Author

• Dharshika Malwane, CUNY Graduate CenterFollow

Date of Degree

6-2026

Document Type

Doctoral Dissertation

Degree Name

Doctor of Philosophy

Program

Physics

Advisor

Karl G. Sandeman

Advisor

Ronald L. Koder

Committee Members

Richard J. Wittebort

Ruth E. Stark

Nicolas Giovambattista

Subject Categories

Biological and Chemical Physics | Engineering Physics | Other Physics | Polymer Chemistry

Keywords

Elastin, Elastocalorics, Biopolymer, Solid-State Cooling, High-Yield Protein Expression, Field-Cycling NMR

Abstract

This thesis investigates elastin as a potential protein-based elastocaloric material for solid-state cooling near room temperature. After outlining the growing need for alternative cooling technologies and the thermodynamic basis of elastocaloric cooling, the work evaluates native elastin using key caloric metrics, including isothermal entropy change (ΔS_iso), adiabatic temperature change (ΔT_ad), refrigerant capacity (RC), and coefficient of performance (COP). Native elastin exhibits a measurable elastocaloric response, with a maximum ΔS_iso of 4.8 J /kg∙K, a maximum indirect ΔT_ad of 0.52 °C, a maximum direct ΔT_ad of 0.21 °C, an RC of 92 J /kg, and a COP of 86. Although these values, except for COP, remain modest relative to leading elastocaloric materials, elastin offers significant advantages, including high extensibility, high fatigue resistance, and low hysteresis.

To explore how this newly reported caloric behavior might be improved, this thesis then investigates the engineering of elastin-inspired materials through the design of a model mini-elastin, the development of a scalable recombinant expression and purification protocol, structural characterization by NMR, and initial efforts toward functional elastomer formation. The mini-elastin construct is purified at a high yield of 850 mg/L culture, establishing a practical route for iterative materials design and testing. Structural analysis further shows that the construct remains highly disordered, supporting the view that intrinsic disorder is central to elastin’s thermomechanical behavior. Overall, this work identifies elastin as a biologically derived caloric platform whose response arises from the coupling of hydrophobic hydration and chain disorder, and it establishes a foundation for the future development of sequence-engineered, protein-based elastocaloric materials.

Recommended Citation

Malwane, Dharshika, "Exploring Native and Designed Elastins as Protein-Based Elastocaloric Materials: A First Investigation" (2026). CUNY Academic Works.
https://academicworks.cuny.edu/gc_etds/6683