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<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">meat</journal-id><journal-title-group><journal-title xml:lang="en">Theory and practice of meat processing</journal-title><trans-title-group xml:lang="ru"><trans-title>Теория и практика переработки мяса</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">2414-438X</issn><issn pub-type="epub">2414-441X</issn><publisher><publisher-name>ФГБНУ «Федеральный научный центр пищевых систем им. В.М. Горбатова» РАН</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.21323/2414-438X-2022-7-4-258-264</article-id><article-id custom-type="elpub" pub-id-type="custom">meat-236</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>Статьи</subject></subj-group></article-categories><title-group><article-title>Biotechnological techniques for intensification of protein extraction from the porcine pancreas</article-title><trans-title-group xml:lang="ru"><trans-title></trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0003-1864-8115</contrib-id><name-alternatives><name name-style="western" xml:lang="en"><surname>Kotenkova</surname><given-names>E. A.</given-names></name></name-alternatives><bio xml:lang="en"><p>Elena A. Kotenkova, Candidate of Technical Sciences, Senior Researcher, Experimental Clinic — Research Laboratory of Biologically Active Substances of an Animal Origin</p><p>26, Talalikhina str., 109316, Moscow</p></bio><email xlink:type="simple">lazovlena92@yandex.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-0211-8171</contrib-id><name-alternatives><name name-style="western" xml:lang="en"><surname>Akhremko</surname><given-names>A. G.</given-names></name></name-alternatives><bio xml:lang="en"><p>Anastasiya G. Akhremko, Candidate of Technical Sciences, Junior Researcher, Experimental Clinic — Research Laboratory of Biologically Active Substances of an Animal Origin</p><p>26, Talalikhina str., 109316, Moscow</p></bio><email xlink:type="simple">a.ahremko@fncps.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0003-2719-9649</contrib-id><name-alternatives><name name-style="western" xml:lang="en"><surname>Polishchuk</surname><given-names>E. K.</given-names></name></name-alternatives><bio xml:lang="en"><p>Ekaterina K. Polishchuk, Research Engineer, Experimental Clinic — Research Laboratory of Biologically Active Substances of an Animal Origin</p><p>26, Talalikhina str., 109316, Moscow</p></bio><email xlink:type="simple">e.politchuk@fncps.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-6886-496X</contrib-id><name-alternatives><name name-style="western" xml:lang="en"><surname>Aryuzina</surname><given-names>M. A.</given-names></name></name-alternatives><bio xml:lang="en"><p>Marina A. Aryuzina, Senior Laboratory Assistant, Experimental Clinic — Research Laboratory of Biologically Active Substances of an Animal Origin</p><p>26, Talalikhina str., 109316, Moscow</p></bio><email xlink:type="simple">m.aryuzina@fncps.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0003-4544-4433</contrib-id><name-alternatives><name name-style="western" xml:lang="en"><surname>Spirina</surname><given-names>M. E.</given-names></name></name-alternatives><bio xml:lang="en"><p>Mariya E.  Spirina, Senior laboratory assistant, Experimental Clinic — Research Laboratory of Biologically Active Substances of an Animal Origin</p><p>26, Talalikhina str., 109316, Moscow</p></bio><email xlink:type="simple">m.spirina@fncps.ru</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff xml:lang="en" id="aff-1"><institution>V. M. Gorbatov Federal Research Center for Food Systems</institution><country>Russian Federation</country></aff><pub-date pub-type="collection"><year>2022</year></pub-date><pub-date pub-type="epub"><day>27</day><month>12</month><year>2022</year></pub-date><volume>7</volume><issue>4</issue><fpage>258</fpage><lpage>264</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Kotenkova E.A., Akhremko A.G., Polishchuk E.K., Aryuzina M.A., Spirina M.E., 2022</copyright-statement><copyright-year>2022</copyright-year><copyright-holder xml:lang="ru">Kotenkova E.A., Akhremko A.G., Polishchuk E.K., Aryuzina M.A., Spirina M.E.</copyright-holder><copyright-holder xml:lang="en">Kotenkova E.A., Akhremko A.G., Polishchuk E.K., Aryuzina M.A., Spirina M.E.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://www.meatjournal.ru/jour/article/view/236">https://www.meatjournal.ru/jour/article/view/236</self-uri><abstract><p>Processing of secondary products after slaughter of farm animals is in demand. The pancreas is a rich source of bioactive protein substances, effective extraction of which is a serious problem today due to their aggregation. The aim of the work was to assess the extractivity of protein substances of the porcine pancreas using sodium chloride, trehalose, arginine, and combination of glycine and proline. The protein concentration was determined in the obtained extracts by the biuret reaction and their protein composition was assessed by densitometry of two-dimensional electropherograms using software ImageMaster™ 2D Platinum powered by Melanie 8.0. The results showed a positive effect of anti-aggregation agents on the release of protein substances into a solution. The highest protein concentration (33.36±0.64 g/l) was observed when adding 1М L-arginine; however, it was conditioned mainly by an increase in the content of three major protein fractions rather than by diversity of the protein composition. In general, the use of 0.9% NaCl as an extractive agent was quite effective, but selectivity to certain protein groups was observed for anti-aggregation agents such as sodium chloride, trehalose, arginine, glycine and proline, as well as their combination. The obtained results are important for intensifying extraction of protein substances including target ones with the subsequent application in different fields.</p></abstract><kwd-group xml:lang="en"><kwd>aggregation</kwd><kwd>anti-aggregation agent</kwd><kwd>extraction</kwd><kwd>protein</kwd><kwd>2-DE</kwd><kwd>trehalose</kwd><kwd>arginine</kwd><kwd>glycine</kwd><kwd>proline</kwd></kwd-group><funding-group><funding-statement xml:lang="en">The article was published as part of the research topic No. FNEN-2019–0008 of the state assignment of the V. M. Gorbatov Federal Research Center for Food Systems of RAS</funding-statement></funding-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Alao, B., Falowo, A., Chulayo, A., Muchenje, V. (2017). The potential of animal by-products in food systems: Production, prospects and challenges. Sustainability (Switzerland), 9(7), Article 1089. https://doi.org/10.3390/su9071089</mixed-citation><mixed-citation xml:lang="en">Alao, B., Falowo, A., Chulayo, A., Muchenje, V. (2017). The potential of animal by-products in food systems: Production, prospects and challenges. Sustainability (Switzerland), 9(7), Article 1089. https://doi.org/10.3390/su9071089</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Marti, D. L., Johnson, R. J., Mathews, K. H. Jr. (2011). Where’s the (Not) Meat? Byproducts From Beef and Pork Production. Retrieved from https://www.ers.usda.gov/webdocs/outlooks/37427/8801_ldpm20901.pdf. Accessed October 3, 2022.</mixed-citation><mixed-citation xml:lang="en">Marti, D. L., Johnson, R. J., Mathews, K. H. Jr. (2011). Where’s the (Not) Meat? Byproducts From Beef and Pork Production. Retrieved from https://www.ers.usda.gov/webdocs/outlooks/37427/8801_ldpm20901.pdf. Accessed October 3, 2022.</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Jayathilakan, K., Sultana, K., Radhakrishna, K., Bawa, A.S. (2012). Utilization of byproducts and waste materials from meat, poultry and fish processing industries: a review. Journal of Food Science and Technology, 49(3), 278–293. https://doi.org/10.1007/s13197–011–0290–7</mixed-citation><mixed-citation xml:lang="en">Jayathilakan, K., Sultana, K., Radhakrishna, K., Bawa, A.S. (2012). Utilization of byproducts and waste materials from meat, poultry and fish processing industries: a review. Journal of Food Science and Technology, 49(3), 278–293. https://doi.org/10.1007/s13197–011–0290–7</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Nasonova, V. V. (2018). Perspective ways the use of byproducts. Theory and Practice of Meat Processing, 3(3), 64–73. https://doi.org/10.21323/2414–438X-2018–3–3–64–73</mixed-citation><mixed-citation xml:lang="en">Nasonova, V. V. (2018). Perspective ways the use of byproducts. Theory and Practice of Meat Processing, 3(3), 64–73. https://doi.org/10.21323/2414–438X-2018–3–3–64–73</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Velenturf, A. P. M., Purnell, P. (2021). Principles for a sustainable circular economy. Sustainable Production and Consumption, 27, 1437–1457. https://doi.org/10.1016/j.spc.2021.02.018</mixed-citation><mixed-citation xml:lang="en">Velenturf, A. P. M., Purnell, P. (2021). Principles for a sustainable circular economy. Sustainable Production and Consumption, 27, 1437–1457. https://doi.org/10.1016/j.spc.2021.02.018</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Ladisch, M. R., Kohlmann, K. L. (1992). Recombinant human insulin. Biotechnology Progress, 8(6), 469–478. https://doi.org/10.1021/bp00018a001</mixed-citation><mixed-citation xml:lang="en">Ladisch, M. R., Kohlmann, K. L. (1992). Recombinant human insulin. Biotechnology Progress, 8(6), 469–478. https://doi.org/10.1021/bp00018a001</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Siew, Y. Y., Zhang, W. (2021). Downstream processing of recombinant human insulin and its analogues production from E. coli inclusion bodies. Bioresources and Bioprocessing, 8(1), Article 65. https://doi.org/10.1186/s40643–021–00419-w</mixed-citation><mixed-citation xml:lang="en">Siew, Y. Y., Zhang, W. (2021). Downstream processing of recombinant human insulin and its analogues production from E. coli inclusion bodies. Bioresources and Bioprocessing, 8(1), Article 65. https://doi.org/10.1186/s40643–021–00419-w</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">UniProt Protein Database (2022). Retrieved from http://www.uniprot.org/. Accessed July 3, 2022.</mixed-citation><mixed-citation xml:lang="en">UniProt Protein Database (2022). Retrieved from http://www.uniprot.org/. Accessed July 3, 2022.</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Vasilevskaya, E. R., Aryuzina, M. A., Vetrova, E. S. (2021). Comparative study of technologies for extraction of biologically active substances from the raw material of animal origin. Theory and Practice of Meat Processing, 6(3), 226–235. https://doi.org/10.21323/2414–438X-2021–6–3–226–235</mixed-citation><mixed-citation xml:lang="en">Vasilevskaya, E. R., Aryuzina, M. A., Vetrova, E. S. (2021). Comparative study of technologies for extraction of biologically active substances from the raw material of animal origin. Theory and Practice of Meat Processing, 6(3), 226–235. https://doi.org/10.21323/2414–438X-2021–6–3–226–235</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Dobson, C. M. (2004). Principles of protein folding, misfolding and aggregation. Seminars in Cell and Developmental Biology, 15(1), 3–16. https://doi.org/10.1016/j.semcdb.2003.12.008</mixed-citation><mixed-citation xml:lang="en">Dobson, C. M. (2004). Principles of protein folding, misfolding and aggregation. Seminars in Cell and Developmental Biology, 15(1), 3–16. https://doi.org/10.1016/j.semcdb.2003.12.008</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Wang, W., Nema, S., Teagarden, D. (2010). Protein aggregation — Pathways and influencing factors. International Journal of Pharmaceutics, 390(2), 89–99. https://doi.org/10.1016/j.ijpharm.2010.02.025</mixed-citation><mixed-citation xml:lang="en">Wang, W., Nema, S., Teagarden, D. (2010). Protein aggregation — Pathways and influencing factors. International Journal of Pharmaceutics, 390(2), 89–99. https://doi.org/10.1016/j.ijpharm.2010.02.025</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Alam, P., Siddiqi, K., Chturvedi, S. K., Khan, R. H. (2017). Protein aggregation: From background to inhibition strategies. International Journal of Biological Macromolecules, 103, 208–219. https://doi.org/10.1016/j.ijbiomac.2017.05.048</mixed-citation><mixed-citation xml:lang="en">Alam, P., Siddiqi, K., Chturvedi, S. K., Khan, R. H. (2017). Protein aggregation: From background to inhibition strategies. International Journal of Biological Macromolecules, 103, 208–219. https://doi.org/10.1016/j.ijbiomac.2017.05.048</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Hamada, H., Arakawa, T., Shiraki, K. (2009). Effect of additives on protein aggregation. Current Pharmaceutical Biotechnology, 10(4), 400–407. https://doi.org/10.2174/138920109788488941</mixed-citation><mixed-citation xml:lang="en">Hamada, H., Arakawa, T., Shiraki, K. (2009). Effect of additives on protein aggregation. Current Pharmaceutical Biotechnology, 10(4), 400–407. https://doi.org/10.2174/138920109788488941</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Akhremko, A., Vasilevskaya, E. R., Fedulova, L. (2020). Adaptation of two-dimensional electrophoresis for muscle tissue analysis. Potravinarstvo Slovak Journal of Food Sciences, 14, 595– 601. https://doi.org/10.5219/1380</mixed-citation><mixed-citation xml:lang="en">Akhremko, A., Vasilevskaya, E. R., Fedulova, L. (2020). Adaptation of two-dimensional electrophoresis for muscle tissue analysis. Potravinarstvo Slovak Journal of Food Sciences, 14, 595– 601. https://doi.org/10.5219/1380</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Lebendiker, M., Danieli, T. (2014). Production of prone-to-aggregate proteins. FEBS Letters, 588(2), 236–246. https://doi.org/10.1016/j.febslet.2013.10.044</mixed-citation><mixed-citation xml:lang="en">Lebendiker, M., Danieli, T. (2014). Production of prone-to-aggregate proteins. FEBS Letters, 588(2), 236–246. https://doi.org/10.1016/j.febslet.2013.10.044</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Vasilevskaya, E. R., Aryuzina, M. A., Vetrova, E. S. (2021). Saline extraction as a method of obtaining a mixture of biologically active compounds of protein nature from a porcine pancreas. Food Systems, 4(2), 97–105. https://doi.org/10.21323/2618–9771–2020–4–2–97–105 (In Russian)</mixed-citation><mixed-citation xml:lang="en">Vasilevskaya, E. R., Aryuzina, M. A., Vetrova, E. S. (2021). Saline extraction as a method of obtaining a mixture of biologically active compounds of protein nature from a porcine pancreas. Food Systems, 4(2), 97–105. https://doi.org/10.21323/2618–9771–2020–4–2–97–105 (In Russian)</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Bondos, S. E., Bicknell, A. (2003). Detection and prevention of protein aggregation before, during, and after purification. Analytical Biochemistry, 316(2), 223–231. https://doi.org/10.1016/S0003–2697(03)00059–9</mixed-citation><mixed-citation xml:lang="en">Bondos, S. E., Bicknell, A. (2003). Detection and prevention of protein aggregation before, during, and after purification. Analytical Biochemistry, 316(2), 223–231. https://doi.org/10.1016/S0003–2697(03)00059–9</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Li, J., Chen, J., An, L., Yuan, X., Yao, L. (2020). Polyol and sugar osmolytes can shorten protein hydrogen bonds to modulate function. Communications Biology, 3(1), Article 528. https://doi.org/10.1038/s42003–020–01260–1</mixed-citation><mixed-citation xml:lang="en">Li, J., Chen, J., An, L., Yuan, X., Yao, L. (2020). Polyol and sugar osmolytes can shorten protein hydrogen bonds to modulate function. Communications Biology, 3(1), Article 528. https://doi.org/10.1038/s42003–020–01260–1</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Schein, C. H. (1990). Solubility as a function of protein structure and solvent components. Nature Biotechnology, 8(4), 308– 317. https://doi.org/10.1038/nbt0490–308</mixed-citation><mixed-citation xml:lang="en">Schein, C. H. (1990). Solubility as a function of protein structure and solvent components. Nature Biotechnology, 8(4), 308– 317. https://doi.org/10.1038/nbt0490–308</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Jain, N. K., Roy, I. (2008). Effect of trehalose on protein structure. Protein Science, 18(1), 24–36. https://doi.org/10.1002/pro.3</mixed-citation><mixed-citation xml:lang="en">Jain, N. K., Roy, I. (2008). Effect of trehalose on protein structure. Protein Science, 18(1), 24–36. https://doi.org/10.1002/pro.3</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Olsson, C., Swenson, J. (2019). The role of disaccharides for protein–protein interactions — a SANS study. Molecular Physics, 117(22), 3408–3416. https://doi.org/10.1080/00268976.2019.1640400</mixed-citation><mixed-citation xml:lang="en">Olsson, C., Swenson, J. (2019). The role of disaccharides for protein–protein interactions — a SANS study. Molecular Physics, 117(22), 3408–3416. https://doi.org/10.1080/00268976.2019.1640400</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Das, U., Hariprasad, G., Ethayathulla, A.S., Manral, P., Das, T.K., Pasha, S. et al. (2007). Inhibition of protein aggregation: Supramolecular assemblies of arginine hold the key. PLoS ONE, 2(11), Article e1176. https://doi.org/10.1371/journal.pone.0001176</mixed-citation><mixed-citation xml:lang="en">Das, U., Hariprasad, G., Ethayathulla, A.S., Manral, P., Das, T.K., Pasha, S. et al. (2007). Inhibition of protein aggregation: Supramolecular assemblies of arginine hold the key. PLoS ONE, 2(11), Article e1176. https://doi.org/10.1371/journal.pone.0001176</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Tsumoto, K., Umetsu, M., Kumagai, I., Ejima, D., Philo, J.S., Arakawa, T. (2004). Role of arginine in protein refolding, solubilization, and purification. Biotechnology Progress, 20(5), 1301– 1308. https://doi.org/10.1021/bp0498793</mixed-citation><mixed-citation xml:lang="en">Tsumoto, K., Umetsu, M., Kumagai, I., Ejima, D., Philo, J.S., Arakawa, T. (2004). Role of arginine in protein refolding, solubilization, and purification. Biotechnology Progress, 20(5), 1301– 1308. https://doi.org/10.1021/bp0498793</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Shiraki, K., Kudou, M., Fujiwara, S., Imanaka, T., Takagi, M. (2002). Biophysical effect of amino acids on the prevention of protein aggregation. Journal of Biochemistry, 132(4), 591–595. https://doi.org/10.1093/oxfordjournals.jbchem.a003261</mixed-citation><mixed-citation xml:lang="en">Shiraki, K., Kudou, M., Fujiwara, S., Imanaka, T., Takagi, M. (2002). Biophysical effect of amino acids on the prevention of protein aggregation. Journal of Biochemistry, 132(4), 591–595. https://doi.org/10.1093/oxfordjournals.jbchem.a003261</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Platts, L., Falconer, R. J. (2015). Controlling protein stability: Mechanisms revealed using formulations of arginine, glycine and guanidinium HCl with three globular proteins. International Journal of Pharmaceutics, 486(1–2), 131–135. https://doi.org/10.1016/j.ijpharm.2015.03.051</mixed-citation><mixed-citation xml:lang="en">Platts, L., Falconer, R. J. (2015). Controlling protein stability: Mechanisms revealed using formulations of arginine, glycine and guanidinium HCl with three globular proteins. International Journal of Pharmaceutics, 486(1–2), 131–135. https://doi.org/10.1016/j.ijpharm.2015.03.051</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Rajan, R., Ahmed, S., Sharma, N., Kumar, N., Debas, A., Matsumura, K. (2021). Review of the current state of protein aggregation inhibition from a materials chemistry perspective: special focus on polymeric materials. Materials Advances, 2(4), 1139– 1176. https://doi.org/10.1039/D0MA00760A</mixed-citation><mixed-citation xml:lang="en">Rajan, R., Ahmed, S., Sharma, N., Kumar, N., Debas, A., Matsumura, K. (2021). Review of the current state of protein aggregation inhibition from a materials chemistry perspective: special focus on polymeric materials. Materials Advances, 2(4), 1139– 1176. https://doi.org/10.1039/D0MA00760A</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
