Designer Protein-Based Performance Materials

Abstract

Repeat sequence protein polymer (RSPP) technology provides a platform to design and make protein-based performance polymers and represents the best nature has to offer. We report here that the RSPP platform is a novel approach to produce functional protein polymers that have both biomechanical and biofunctional blocks built into one molecule by design, using peptide motifs. We have shown that protein-based designer biopolymers can be made using recombinant DNA technology and fermentation and offer the ability to screen for desired properties utilizing the tremendous potential diversity of amino acid combinations. The technology also allows for large-scale manufacturing with a favorable fermentative cost-structure to deliver commercially viable performance polymers. Using three diverse examples with antimicrobial, textile targeting, and UV-protective agent, we have introduced functional attributes into structural protein polymers and shown, for example, that the functionalized RSPPs have possible applications in biodefense, industrial biotechnology, and personal care areas. This new class of biobased materials will simulate natural biomaterials that can be modified for desired function and have many advantages over conventional petroleum-based polymers.

Design of Disulfide-linked Thioredoxin Dimers and Multimers Through Analysis of Crystal Contacts

“…Designed repeat sequence protein polymers can be isolated to obtain performance materials having both biomechanical and biofunctional blocks built into one molecule, and these could have applications in biodefence, industrial biotechnology and personal care areas. 31 High molecular mass protein polymers can be designed to self-assemble in solution to form transparent, selfsupporting gels that have a high degree of elasticity. 32 A disulfide-bridged protein polymer of α s1 -casein was constructed by chemical introduction of thiol groups into its lysine residues.…”

Genetic Engineering of Self-Assembled Protein Hydrogel Based on Elastin-like Sequences with Metal Binding Functionality

“…Prior to measurements, each sample was diluted by adding water to the appropriate dilutions. In addition, the metal binding capability of free triblock copolymer in aqueous solution as well as (His) 6 (VPGVG) 78 (His) 6 constructed previously 11 were examined. Ten nanomoles of biopolymers was used in the experiments, and the same procedures were performed.…”

“…4 Because of the sequence-directed control over structure and property as well as their intrinsic stimuli-responsive selfassembly capability, protein copolymers based on ELP sequences have been attracting attention as novel biomaterials. 6 A logical extension in expanding the types of application is to introduce additional functionalities into this self-assembled peptide system. Previously, we have demonstrated that ELPs can be engineered to integrate multifunctionalities while preserving the phase-transition property.…”

“…The Maximum (Equilibrium) Cd 2+ Binding Capacity for 10 wt % PE1.6 Hydrogel, Free PE1.6 Copolymer Solution and (His) 6 (VPGVG) 78 (His)6 Biopolymers in TB8 after Overnight Incubation a The latter two biopolymers bound to Cd 2+ were recovered through temperature-induced phase separation.…”

Synthesis of Genes with Multiple Identical Domains

“…A set of overlapping primers will reconstitute the desired gene in a two-step PCR method known as gene assembly or gene synthesis (1,2). However, for genes with multiple identical domains or internal sequence repeats, which have gained increased interest as models for repeat proteins (3,4) and as designed proteins (5), this method of gene synthesis may fail due to mispriming. This drawback might be avoided by synthesis of alternative primers for each domain due to the degenerated genetic code (6), but with increasing numbers of domains, the variability of the oligonucleotides will be exhausted.…”