Abstract
Elastomeric proteins have evolved independently multiple times through evolution. Produced as monomers, they self-assemble into polymeric structures that impart properties of stretch and recoil. They are composed of an alternating domain architecture of elastomeric domains interspersed with cross-linking elements. While the former provide the elasticity as well as help drive the assembly process, the latter serve to stabilise the polymer. Changes in the number and arrangement of the elastomeric and cross-linking regions have been shown to significantly impact their assembly and mechanical properties. However, to date, such studies are relatively limited. Here we present a theoretical study that examines the impact of domain architecture on polymer assembly and integrity. At the core of this study is a novel simulation environment that uses a model of diffusion limited aggregation to simulate the self-assembly of rod-like particles with alternating domain architectures. Applying the model to different domain architectures, we generate a variety of aggregates which are subsequently analysed by graph-theoretic metrics to predict their structural integrity. Our results show that the relative length and number of elastomeric and cross-linking domains can significantly impact the morphology and structural integrity of the resultant polymeric structure. For example, the most highly connected polymers were those constructed from asymmetric rods consisting of relatively large cross-linking elements interspersed with smaller elastomeric domains. In addition to providing insights into the evolution of elastomeric proteins, simulations such as those presented here may prove valuable for the tuneable design of new molecules that may be exploited as useful biomaterials.
Highlights
Elastomeric proteins such as elastin, resilin, abductin, spider dragline silks and wheat gluten represent a remarkable class of selfassembling proteins that provide properties of extensibility and elastic recoil [1]
Each protein appears to have arisen independently: elastin is a vertebrate protein that plays an integral role in the extracellular matrix (ECM) of elastic tissues such as aorta, arteries and lung parenchyma; resilin is found in specialized regions of the cuticle of insects where it functions as an energy store; abductin is located in the hinge region of bivalves, responsible for opening the shell upon relaxation of the abductor muscle; spider dragline silks are used by spiders as safety lines or for constructing the frames of their webs; and gluten is a plant protein that may have evolved to facilitate efficient packaging as a food store for developing seedlings [11]
Natural dragline spider silk proteins analysed to date demonstrate very high molecular weights (250–320 kDa [52,53])
Summary
Elastomeric proteins such as elastin, resilin, abductin, spider dragline silks and wheat gluten represent a remarkable class of selfassembling proteins that provide properties of extensibility and elastic recoil [1]. There has been much interest in their development as mechanically active biomaterials for purposes of tissue replacement and tissue engineering [2,3,4] In addition to their elastomeric properties, their ability to selfassemble suggests a role as scaffolds for tissue engineering with tremendous promise in regenerative medicine [5]. Gluten and resilin are largely composed of repetitive hydrophobic elements interspersed with tyrosine residues, involved in the formation of di- and tri-tyrosine cross links [8,13,14]. It is thought that elastomeric domains are relatively disordered; composed mainly of b-turns and b-strands
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