Title of Oral/Poster Presentation

Novel Methods to Produce Large Recombinant Spider Silk Proteins

Presenter Information

Nathan HebertFollow

Class

Article

Graduation Year

2018

College

College of Engineering

Department

Biological Engineering Department

Faculty Mentor

Dr. Randy Lewis

Presentation Type

Poster Presentation

Abstract

Spider silk has long been an interest of scientific research due to its’ remarkable mechanical properties. Until recently there has been no way to effectively obtain spider silk, except by harvesting it from individual spiders. With advances in technology, the genes that code for the individual spider silk proteins have been isolated and genetically engineered into other hosts to produce recombinant spider silk proteins (rSSps) of varying molecular weights, ranging from 10 kDa to 250 kDa. The larger the rSSps’ molecular weight, the greater the mechanical properties of the ensuing product will be. Unfortunately, when utilizing current production methods, larger molecular weight rSSps cannot be produced in commercially viable quantities while simultaneously maintaining low levels of impurities. Small molecular weight rSSps (10 - 80 kDa) are easier to produce in genetically engineered systems whilst maintaining favorable yields and purities. To alleviate current production constraints, the expression of small molecular weight rSSps can be achieved by utilizing current production methods that result in large quantities of proteins with a high degree of purity. After the small molecular weight rSSps are expressed and purified they are polymerized to form a larger molecular weight rSSps. There are two unique systems that can cause this polymerization via the autocatalytic nature of the Spy System peptides and split inteins. These small molecular weight fusion rSSps are purified and polymerized to form larger molecular weight rSSps that possess the favorable mechanical properties that larger molecular weight rSSps demonstrate. These two systems can be applied to other areas, such as surface binding rSSps or creating tunable chimeric rSSps. By combining rSSps with autocatalytic peptides that can self-assemble, innovative production methods and products can be attained with rSSps while also increasing production yields and purity.

Location

North Atrium

Start Date

13-4-2017 1:30 PM

End Date

13-4-2017 2:45 PM

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Apr 13th, 1:30 PM Apr 13th, 2:45 PM

Novel Methods to Produce Large Recombinant Spider Silk Proteins

North Atrium

Spider silk has long been an interest of scientific research due to its’ remarkable mechanical properties. Until recently there has been no way to effectively obtain spider silk, except by harvesting it from individual spiders. With advances in technology, the genes that code for the individual spider silk proteins have been isolated and genetically engineered into other hosts to produce recombinant spider silk proteins (rSSps) of varying molecular weights, ranging from 10 kDa to 250 kDa. The larger the rSSps’ molecular weight, the greater the mechanical properties of the ensuing product will be. Unfortunately, when utilizing current production methods, larger molecular weight rSSps cannot be produced in commercially viable quantities while simultaneously maintaining low levels of impurities. Small molecular weight rSSps (10 - 80 kDa) are easier to produce in genetically engineered systems whilst maintaining favorable yields and purities. To alleviate current production constraints, the expression of small molecular weight rSSps can be achieved by utilizing current production methods that result in large quantities of proteins with a high degree of purity. After the small molecular weight rSSps are expressed and purified they are polymerized to form a larger molecular weight rSSps. There are two unique systems that can cause this polymerization via the autocatalytic nature of the Spy System peptides and split inteins. These small molecular weight fusion rSSps are purified and polymerized to form larger molecular weight rSSps that possess the favorable mechanical properties that larger molecular weight rSSps demonstrate. These two systems can be applied to other areas, such as surface binding rSSps or creating tunable chimeric rSSps. By combining rSSps with autocatalytic peptides that can self-assemble, innovative production methods and products can be attained with rSSps while also increasing production yields and purity.