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Self-assembling peptides: From a discovery in a yeast protein to diverse uses and beyond.

ABSTRACT: Well-defined nanofiber scaffold hydrogels made of self-assembling peptides have found their way into various 3D tissue culture and clinical products. I reflect initial puzzlement of the unexpected discovery, gradual understanding of how these peptides undergo self-assembly, to eventually translating designer biological scaffolds into commercial products. Peptides are ubiquitous in nature and useful in many fields. They are found as hormones, pheromones, antibacterial, and antifungal agents in innate immunity systems, toxins, as well anti-inset pesticides. However, the concept of peptides as materials was not recognized until 1990 when a self-assembling peptide as a repeating segment in a yeast protein was serendipitously discovered. The peptide materials have bona fide materials properties and are made from simple amino acids with well-ordered nanostructures under physiological conditions. Some current applications include: (a) Real 3D tissue cell cultures of diverse tissue cells and various stem cells; (b) reparative and regenerative medicine as well as tissue engineering; (c) 3D tissue printing; (d) sustained releases of small molecules, growth factors and monoclonal antibodies; and (e) accelerated wound healing of skin and diabetic ulcers as well as instant hemostasis in surgery. Self-assembling peptide nanobiotechnology will likely continue to expand in many directions in the coming years. I will also briefly introduce my current research using a simple QTY code for membrane protein design. I am greatly honored and humbled to be invited to contribute an Award Winner Recollection of the 2020 Emil Thomas Kaiser Award from the Protein Society.

SUBMITTER: Zhang S

PROVIDER: S-EPMC7586918 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:BackgroundProtein purification remains a critical need for biosciences and biotechnology. It frequently requires multiple rounds of chromatographic steps that are expensive and time-consuming. Our lab previously reported a cleavable self-aggregating tag (cSAT) scheme for streamlined protein expression and purification. The tag consists of a self-assembling peptide (SAP) and a controllable self-cleaving intein. The SAP drives the target protein into an active aggregate, then by intein-mediated cleavage, the target protein is released. Here we report a novel cSAT scheme in which the self-assembling peptide is replaced with a salt inducible self-assembling peptide. This allows a target protein to be expressed first in the soluble form, and the addition of salt then drives the target protein into the aggregated form, followed by cleavage and release.ResultsIn this study, we used MpA (MKQLEDKIEELLSKAAMKQLEDKIEELLSK) as a second class of self-assembling peptide in the cSAT scheme. This scheme utilizes low salt concentration to keep the fusion protein soluble, while eliminating insoluble cellular matters by centrifugation. Salt then triggers MpA-mediated self-aggregation of the fusion, removing soluble background host cell proteins. Finally, intein-mediated cleavage releases the target protein into solution. As a proof-of-concept, we successfully purified four proteins and peptides (human growth hormone, 22.1 kDa; LCB3, 7.7 kDa; SpyCatcherΔN-ELP-SpyCatcherΔN, 26.2 kDa; and xylanase, 45.3 kDa) with yields ranging from 12 to 87 mg/L. This was comparable to the classical His-tag method both in yield and purity (72-97%), but without the His-tag. By using a further two-step column purification process that included ion-exchange chromatography and size-exclusion chromatography, the purity was increased to over 99%.ConclusionOur results demonstrate that a salt-inducible self-assembling peptide can serve as a controllable aggregating tag, which might be advantageous in applications where soluble expression of the target protein is preferred. This work also demonstrates the potential and advantages of utilizing salt inducible self-assembling peptides for protein separation.

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Self-assembling peptides: From a discovery in a yeast protein to diverse uses and beyond.

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