Mechanical properties, protein-based materials

Due to the struggle to survive under circumstances of limited food supply, organisms evolve to use the most efficient mechanism available to their composition. The most efficient mechanism available to the proteins that sustain Life would seem to be the apolar-polar repulsive free energy of hydration as observed for the inverse temperature transitions for hydrophobic association. The efficiency of designed elastic-contractile protein-based machines and a number of additional properties make designed protein-based materials of substantial promise for the marketplace of the future. 

Finally, for medical applications, the extraordinary biocompatibility of these elastic protein-based materials, we believe, arises from the specific means whereby these elastic protein-based polymers exhibit their motion. Being composed of repeating peptide sequences that order into regular, nonrandom, dynamic structures, these elastic protein-based polymers exhibit mechanical resonances that present barriers to the approach of antibodies as required to be identified as foreign. In addition, we also believe that these mechanical resonances result in extraordinary absorption properties in the acoustic frequency range. 

The initial preparation of protein-based polymers utilized solution and solid phase peptide chemistry. This made possible the preparation of more than 1,000 polymer compositions. As discussed in Chapter 5, these compositions were studied for determination of their basic properties, for the development of the set of phenomenological axioms for protein engineering and function, and for the demonstration of the basic mechanism that underlies function. In short, it is the chemical synthesis that has allowed development of much of the basic science and the demonstration of the potential of protein-based materials in a timely manner. Mostly because of the historical relevance, but also because of the unique contributions of chemical synthesis to arriving at satisfactory purification of microbially prepared protein-based polymers, a brief description of the chemical synthesis of protein-based polymers is given below. 

ProLastin polymers are a family of protein-based materials w hose resorption rate in vivo can be controlled by adjusting the sequence and not just the composition of the polymer (Cappello et al, 1995). These adjustments can be made so as to cause little change in the formulation characteristics of the materials, their physical forms, or their mechanical properties. They have good mechanical integrity with no need for chemical crosslinking. They degrade by enzymatic proteolysis and are presumed to resorb by surface erosion. Their breakdowm products are peptides or amino acids w hich are electroneutral at physiological pH and cause no undue inflammation or tissue response. 

A downside to the sustainable and extensive use of soy protein-based materials is their intrinsic reactivity and thus lower inertia when compared to most conventional petrochemical-based plastics. They are known to be sensitive to microbial spoilage and also to water due to hydrophilic nature of many amino acids constituting their primary structure and to the substantial amount of hydrophilic plasticizer required to impart thermo-processability and film flexibility. As a consequence, their mechanical properties and water vapor barrier properties in high moisture conditions are poor compared to synthetic films such as low-density polyethylene. 

The mechanical properties of protein-based materials are substantially lower than those of standard synthetic materials, such as polyvinylidene chloride (PVDC) or polyester (Table 11.11). The mechanical properties of protein-based materials were measured and modelled as a function of film characteristics [74, 131, 132]. For stronger materials (e.g., based on wheat gluten, corn gluten and myofibrillar proteins, critical deformation (DC) = 0.7 mm) and elastic modulus (K = 510 N/m) values are slightly lower than those of reference materials such as LDPE (DC = 2.3 mm, K = 135 N/m), cellulose (DC = 3.3 mm, K = 350 N/m) or even PVC films. The mechanical properties of corn gluten-based material are close to those of PVC. 

The mechanical properties of protein-based materials have been studied (Table II) and modeled (9,31-33). 

The mechanical properties of protein-based materials closely depend on the plasticizer content, temperature and ambient relative humidity (16,34,35). At constant temperature and composition, an increase in relative humidity leads to a major change in the material properties, with a sharp drop in mechanical strength and a concomitant sharp rise in distortion. These modifications occur when the Tg of the material is surpassed (Figure 1). These variations can be reduced by implementing crosslinking treatments (physical or chemical) or using high cellulose or mineral loads (22). 

The mechanical properties of protein-based materials can partly be related to the distribution and intensity of inter- and intra-molecular interactions that take place in primary and spatial structures. The cohesion of protein materials mainly depends on the distribution and intensity of intra- and inter-protein interactions, as well as interactions with other components. For example, in soy-based materials, hydrophobic interactions... 

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