Functional composite material for protein purification
(2020) KBKM05 20192Pure and Applied Biochemistry
Computational Chemistry
- Abstract
- The vision of protein purification is to be both efficient and environmentally friendly with the ability of reusage. This project has been focused on designing and synthesizing a functional composite material that can be used for protein purification. The material consists of silica particles coated with polydopamine, an affordable and easy synthesized material that can be reused. The ability of reusage is due to a dynamic bonding between polydopamine and azide modified boronic acid. The azide modified boronic acid is in turn bound to N-propargyl iminodiacetic acid which is a component with a triple bond able to bind a transition metal ion.
This study has been able to prove that a histidine tagged lactate dehydrogenase (LDH) have an... (More) - The vision of protein purification is to be both efficient and environmentally friendly with the ability of reusage. This project has been focused on designing and synthesizing a functional composite material that can be used for protein purification. The material consists of silica particles coated with polydopamine, an affordable and easy synthesized material that can be reused. The ability of reusage is due to a dynamic bonding between polydopamine and azide modified boronic acid. The azide modified boronic acid is in turn bound to N-propargyl iminodiacetic acid which is a component with a triple bond able to bind a transition metal ion.
This study has been able to prove that a histidine tagged lactate dehydrogenase (LDH) have an ability to bind to the transition metal on the synthesized material with an average of 40 mg protein per gram particles without any unspecific binding. No affinity has been showed to non-His-tagged protein. The ability of protein binding to the material has also been proved by measuring the enzyme activity of His-LDH where the specific enzyme activity increased for the eluted proteins compared to the crude protein sample. The silica with coated polydopamine have also been proved to be reusable by replacing the bonding between polydopamine and azide modified boronic acid using fructose molecules. These finding suggest that this material may be promising for protein purification in the future. (Less) - Popular Abstract
- Proteins are macromolecules with different functions in the human body. The process of characterization of proteins is important to study their function and structure but also to determine their amino acid sequence. This is important in the field of example drug development as more knowledge of the protein structure allows for more accurate and efficient treatments. For this to be carried out the proteins needs to be separated from a mixture of other components, for example other proteins. This process is called protein purification.
In this work a material was designed and synthesized to be used for protein purification.
Please use this url to cite or link to this publication:
http://lup.lub.lu.se/student-papers/record/9004317
- author
- el-Sakka, Fardous LU
- supervisor
- organization
- course
- KBKM05 20192
- year
- 2020
- type
- H2 - Master's Degree (Two Years)
- subject
- keywords
- Applied biochemistry, Tillämpad biokemi
- language
- English
- id
- 9004317
- date added to LUP
- 2020-06-12 13:56:54
- date last changed
- 2020-06-12 13:56:54
@misc{9004317, abstract = {{The vision of protein purification is to be both efficient and environmentally friendly with the ability of reusage. This project has been focused on designing and synthesizing a functional composite material that can be used for protein purification. The material consists of silica particles coated with polydopamine, an affordable and easy synthesized material that can be reused. The ability of reusage is due to a dynamic bonding between polydopamine and azide modified boronic acid. The azide modified boronic acid is in turn bound to N-propargyl iminodiacetic acid which is a component with a triple bond able to bind a transition metal ion. This study has been able to prove that a histidine tagged lactate dehydrogenase (LDH) have an ability to bind to the transition metal on the synthesized material with an average of 40 mg protein per gram particles without any unspecific binding. No affinity has been showed to non-His-tagged protein. The ability of protein binding to the material has also been proved by measuring the enzyme activity of His-LDH where the specific enzyme activity increased for the eluted proteins compared to the crude protein sample. The silica with coated polydopamine have also been proved to be reusable by replacing the bonding between polydopamine and azide modified boronic acid using fructose molecules. These finding suggest that this material may be promising for protein purification in the future.}}, author = {{el-Sakka, Fardous}}, language = {{eng}}, note = {{Student Paper}}, title = {{Functional composite material for protein purification}}, year = {{2020}}, }