Terry, M.; Hurtado, A.; Mendoza, C.; Vargas, L.; Davila, I.; Steele, T.; Gonda, A.; Mizrachi, D. Consequences of Immunoglobulin Domain-Containing Protein Retro-Proteins. Preprints2024, 2024061001. https://doi.org/10.20944/preprints202406.1001.v1
APA Style
Terry, M., Hurtado, A., Mendoza, C., Vargas, L., Davila, I., Steele, T., Gonda, A., & Mizrachi, D. (2024). Consequences of Immunoglobulin Domain-Containing Protein Retro-Proteins. Preprints. https://doi.org/10.20944/preprints202406.1001.v1
Chicago/Turabian Style
Terry, M., Amber Gonda and Dario Mizrachi. 2024 "Consequences of Immunoglobulin Domain-Containing Protein Retro-Proteins" Preprints. https://doi.org/10.20944/preprints202406.1001.v1
Abstract
Amino acid sequences of native proteins are generally not palindromic. The protein molecule obtained as a result of reading the amino acid sequence backwards, i.e., a retro-protein, having the same amino acid composition and the same hydrophobicity profile as the native sequence may behave as a different molecule. Here we have used R4, a directed evolution product of Scfv-13, a protein that binds β-galactosidase, and report the properties of the retro-R4 (rR4). rR4 remains a binding protein and its new target is Glutamine-fructose-6-phosphate aminotransferase (GLMS), a native E. coli protein. Additionally, a tight junction immunoglobulin domain- containing membrane protein, junctional adhesion molecule A (JAMA) retro-protein retains the ability to drive cell-cell interactions. Thus, protein engineering suggests a new potential application to retro-proteins of the immunoglobulin superfamily.
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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