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description.html
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<!DOCTYPE html>
<html lang="en" dir="ltr" class="client-nojs">
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<meta charset="UTF-8" />
<title>Description</title>
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<a href="#h2">Previous treatments</a>
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<p>At present, the incorporation of non-natural amino acids has become an important problem that restricts heterologous protein expression. MAP (mussel adhesive protein), a medical adhesive, cannot be mass produced because
of the defect in the ability of aaRS to incorporate L-DOPA into protein. This causes the patient to choose sutures that cause more pain.
</p>
<br>
<p style="font-family: 'font1';font-size: 40px;color: black;text-align: center;margin: 0 auto 20px auto;">
Why do we choose this project?
<br> <br> <br>
</p>
<h1 id="h1" style="font-size: 25px;">Background
</h1>
<p>MAP, a kind of protein complex secreted by mussel foot glands, is often used as biomedical adhesives because of its strong adhesion, good biodegradability and excellent biocompatibility. Therefore, they have a wide range
of prospects in medical and other industries<sup>1,2</sup>. L-3,4-Dihydroxyphenylalanine (L-DOPA), a noncanonical amino acid formed by hydroxylation of tyrosine, is widely distributed in natural MAPs, acting as a key
factor for adhesion
<sup>3,4</sup>. With the development of the medical industry, the demand for MAPs is rising. However, the extraction of natural MAPs is costly and inefficient. And thus microbial heterologous expression has become one
of the most important ways to produce this protein on a large scale<sup>5</sup>.
</p>
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<img src="./image/design10.png" style="width: 80%;"><br />
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<p>However, the natural aaRS cannot correctly increase L-DOPA into the protein, resulting in the loss of adhesion of MAPs producted by <i>E. coli</i>. Therefore, and we try to make aaRS more efficient and specific to recognize
L-DOPA using directed evolution strategies.
</p>
<div style="display: flex;justify-content: center;align-items: center;">
<img src="./image/2 (2).png" style="width: 430px;height: 500px;">
</div>
<h1 id="h2" style="font-size: 25px;">Previous treatments
</h1>
<p>
Researchers have used many strategies to incorporate L-DOPA into MAPs. For example, Yang and co-workers used a tyrosine-auxotrophy strain to make endogenous TyrRS recognize the L-DOPA as much as possible by reducing one of the substrates of the TyrRS---tyrosine<sup>6</sup>.
The orthogonal translation system is appropriate for directly incorporating noncanonical amino acids such as L-DOPA<sup>7</sup>. Jeong and co-workers used Methanococcus jannaschii TyrRS (MjTyrRS) to incorporate L-DOPA
at a given stop codon to increase L-DOPA in MAPs<sup>8</sup>. However, due to the similarity between tyrosine and L-DOPA in structure, MjTyrRS cannot distinguish them well, which limits the efficiency of L-DOPA incorporation.
</p>
<h1 id="h3" style="font-size: 25px;">Our goal
</h1>
<p>Therefore, we start with MjTyrRS-Gen 2<sup>9</sup> (hereinafter referred to as "Gen 2"), an engineered TyrRS with improved L-DOPA-incorporating activity. And we try to make Gen 2 more efficient and specific to recognize
L-DOPA using directed evolution strategies.
</p>
</div>
<div id="h4" style="text-align:left;">
<h1 style="text-align:left;font-size: 25px;line-height: 30px; ">Reference
</h1>
<p style="text-indent: 0em;">
1 M. J. Harrington, A. Masic, N. Holten-Andersen, J. H. Waite, P. Fratzl, Iron-clad fibers: A metal-based biological strategy for hard flexible coatings. Science 328, 216-220 (2010). <br />https://10. 1126/science.
1181044
</p>
<p style="text-indent: 0em;">2 J. Dove, P. Sheridan, Adhesive protein from mussels - possibilities for dentistry, medicine, and industry. Journal of the American Dental Association 112, 879-879 (1986).
</p>
<p style="text-indent: 0em;"> 3 J. H. Waite, Evidence for a repeating 3,4-dihydroxyphenylalanine- and hydroxyproline-containing decapeptide in the adhesive protein of the mussel, mytilus edulis l. The Journal of biological chemistry 258, 2911-2915 (1983).
</p>
<p style="text-indent: 0em;"> 4 M. E. Yu, J. Y. Hwang, T. J. Deming, Role of l-3,4-dihydroxyphenylalanine in mussel adhesive proteins. Journal of the American Chemical Society 121, 5825-5826 (1999).<br /> https://10. 1021/ja990469y
</p>
<p style="text-indent: 0em;"> 5 Xue Rui, Yao Lin, Wang Rui et al, Advances and Applications of Recombinant Mussel Foot Proteins. China Biotechnology 40, 82-89 (2020). <br />https://10. 13523/j. cb. 2007046
</p>
<p style="text-indent: 0em;">6 B. Yang, N. Ayyadurai, H. Yun et al, In vivo residue-specific dopa-incorporated engineered mussel bioglue with enhanced adhesion and water resistance. Angewandte Chemie-International Edition 53, 13360-13364 (2014). <br
/>https://10. 1002/anie. 201406099
</p>
<p style="text-indent: 0em;">7 S. Smolskaya, Y. A. Andreev, Site-specific incorporation of unnatural amino acids into escherichia coli recombinant protein: Methodology development and recent achievement. Biomolecules 9, (2019).<br /> https://10. 3390/biom9070255
</p>
<p style="text-indent: 0em;">8 Y. S. Jeong, B. Yang, B. Yang et al, Enhanced production of dopa-incorporated mussel adhesive protein using engineered translational machineries. Biotechnology and Bioengineering 117, 1961-1969 (2020).<br /> https://10.
1002/bit. 27339
</p>
<p style="text-indent: 0em;">9 R. Thyer, S. d'Oelsnitz, M. S. Blevins et al, Directed evolution of an improved aminoacyl-trna synthetase for incorporation of l-3,4-dihydroxyphenylalanine (l-dopa). Angewandte Chemie-International Edition 60, 14811-14816
(2021). <br />https://10. 1002/anie. 202100579
</p>
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