Rational Design and Production of Bioactive Analogs of Recombinant Human Keratinocyte Growth Factor (rhKGF) with Reduced Aggregation Propensity
Recombinant human keratinocyte growth factor (rhKGF) is a highly aggregation-prone therapeutic protein. The present study aimed to reduce aggregation propensity of rhKGF by engineering the aggregation hotspots. Initially, 21 mutants were designed based on the previously-identified aggregation-prone...
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| Veröffentlicht in: | The Protein Journal 2023-02, Vol.42 (1), p.37-54 |
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| creator | Dastjerdeh, Mansoureh Shahbazi Yasami-Khiabani, Setayesh Boroujeni, Mohammadtaghi Borjian Shokrgozar, MohammadAli Aliabadi, Hooman Aghamirza Moghim Golkar, Majid Rahimi, Hamzeh |
| description | Recombinant human keratinocyte growth factor (rhKGF) is a highly aggregation-prone therapeutic protein. The present study aimed to reduce aggregation propensity of rhKGF by engineering the aggregation hotspots. Initially, 21 mutants were designed based on the previously-identified aggregation-prone regions (APRs) and then four of them including mutants No. 4 (L91K, I119K), 7 (V13S, L91K), 14 (L91D, I119D), and 21 (A51E) were selected based on molecular dynamics (MD) simulations for further experimental studies. The recombinantly produced rhKGF and mutants were analyzed regarding secondary structure, thermal stability, aggregation propensity, and biological activity. Far-UV CD spectroscopy showed that the mutants have similar secondary structure with rhKGF. A51E mutant showed enhanced stability and decreased monomer loss under heat stress suggesting its reduced aggregation propensity compared to rhKGF. Mutant No. 14 showed higher stability and less aggregation tendency than mutant No. 4 indicating that only mutations decreasing p
I
of rhKGF are effective in reducing its aggregation tendency. All of the mutants were at least as potent as rhKGF in stimulating proliferation of MCF-7 epithelial cells. Our results identified A51E as an equally potent, more stable, and less aggregation-prone analog of rhKGF which could be a promising alternative drug candidate for the commercially available rhKGF (Palifermin). |
| doi_str_mv | 10.1007/s10930-023-10089-6 |
| format | Article |
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I
of rhKGF are effective in reducing its aggregation tendency. All of the mutants were at least as potent as rhKGF in stimulating proliferation of MCF-7 epithelial cells. Our results identified A51E as an equally potent, more stable, and less aggregation-prone analog of rhKGF which could be a promising alternative drug candidate for the commercially available rhKGF (Palifermin).</description><identifier>ISSN: 1572-3887</identifier><identifier>EISSN: 1875-8355</identifier><identifier>EISSN: 1573-4943</identifier><identifier>DOI: 10.1007/s10930-023-10089-6</identifier><identifier>PMID: 36683078</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Agglomeration ; Analysis ; Animal Anatomy ; Biochemistry ; Biological activity ; Bioorganic Chemistry ; Cell proliferation ; Chemistry ; Chemistry and Materials Science ; Drug development ; Epithelial cells ; Epithelium ; Fibroblast Growth Factor 7 ; Growth factors ; Health aspects ; Heat stress ; Heat tolerance ; Histology ; Humans ; Keratinocyte growth factor ; Molecular dynamics ; Molecular Dynamics Simulation ; Morphology ; Mutants ; Mutation ; Organic Chemistry ; Palifermin ; Production management ; Protein structure ; Secondary structure ; Spectroscopy ; Stability analysis ; Structural stability ; Thermal stability</subject><ispartof>The Protein Journal, 2023-02, Vol.42 (1), p.37-54</ispartof><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2023. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.</rights><rights>COPYRIGHT 2023 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c393t-f334ba2ffc5c9f05e19aec9718e37cc28c7e5ea4dc8e12c3b9ce9ccf52d2973f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10930-023-10089-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10930-023-10089-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36683078$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dastjerdeh, Mansoureh Shahbazi</creatorcontrib><creatorcontrib>Yasami-Khiabani, Setayesh</creatorcontrib><creatorcontrib>Boroujeni, Mohammadtaghi Borjian</creatorcontrib><creatorcontrib>Shokrgozar, MohammadAli</creatorcontrib><creatorcontrib>Aliabadi, Hooman Aghamirza Moghim</creatorcontrib><creatorcontrib>Golkar, Majid</creatorcontrib><creatorcontrib>Rahimi, Hamzeh</creatorcontrib><title>Rational Design and Production of Bioactive Analogs of Recombinant Human Keratinocyte Growth Factor (rhKGF) with Reduced Aggregation Propensity</title><title>The Protein Journal</title><addtitle>Protein J</addtitle><addtitle>Protein J</addtitle><description>Recombinant human keratinocyte growth factor (rhKGF) is a highly aggregation-prone therapeutic protein. The present study aimed to reduce aggregation propensity of rhKGF by engineering the aggregation hotspots. Initially, 21 mutants were designed based on the previously-identified aggregation-prone regions (APRs) and then four of them including mutants No. 4 (L91K, I119K), 7 (V13S, L91K), 14 (L91D, I119D), and 21 (A51E) were selected based on molecular dynamics (MD) simulations for further experimental studies. The recombinantly produced rhKGF and mutants were analyzed regarding secondary structure, thermal stability, aggregation propensity, and biological activity. Far-UV CD spectroscopy showed that the mutants have similar secondary structure with rhKGF. A51E mutant showed enhanced stability and decreased monomer loss under heat stress suggesting its reduced aggregation propensity compared to rhKGF. Mutant No. 14 showed higher stability and less aggregation tendency than mutant No. 4 indicating that only mutations decreasing p
I
of rhKGF are effective in reducing its aggregation tendency. All of the mutants were at least as potent as rhKGF in stimulating proliferation of MCF-7 epithelial cells. Our results identified A51E as an equally potent, more stable, and less aggregation-prone analog of rhKGF which could be a promising alternative drug candidate for the commercially available rhKGF (Palifermin).</description><subject>Agglomeration</subject><subject>Analysis</subject><subject>Animal Anatomy</subject><subject>Biochemistry</subject><subject>Biological activity</subject><subject>Bioorganic Chemistry</subject><subject>Cell proliferation</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Drug development</subject><subject>Epithelial cells</subject><subject>Epithelium</subject><subject>Fibroblast Growth Factor 7</subject><subject>Growth factors</subject><subject>Health aspects</subject><subject>Heat stress</subject><subject>Heat tolerance</subject><subject>Histology</subject><subject>Humans</subject><subject>Keratinocyte growth factor</subject><subject>Molecular dynamics</subject><subject>Molecular Dynamics 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Design and Production of Bioactive Analogs of Recombinant Human Keratinocyte Growth Factor (rhKGF) with Reduced Aggregation Propensity</title><author>Dastjerdeh, Mansoureh Shahbazi ; Yasami-Khiabani, Setayesh ; Boroujeni, Mohammadtaghi Borjian ; Shokrgozar, MohammadAli ; Aliabadi, Hooman Aghamirza Moghim ; Golkar, Majid ; Rahimi, Hamzeh</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-f334ba2ffc5c9f05e19aec9718e37cc28c7e5ea4dc8e12c3b9ce9ccf52d2973f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Agglomeration</topic><topic>Analysis</topic><topic>Animal Anatomy</topic><topic>Biochemistry</topic><topic>Biological activity</topic><topic>Bioorganic Chemistry</topic><topic>Cell proliferation</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Drug development</topic><topic>Epithelial cells</topic><topic>Epithelium</topic><topic>Fibroblast Growth Factor 7</topic><topic>Growth factors</topic><topic>Health aspects</topic><topic>Heat stress</topic><topic>Heat tolerance</topic><topic>Histology</topic><topic>Humans</topic><topic>Keratinocyte growth factor</topic><topic>Molecular dynamics</topic><topic>Molecular Dynamics Simulation</topic><topic>Morphology</topic><topic>Mutants</topic><topic>Mutation</topic><topic>Organic Chemistry</topic><topic>Palifermin</topic><topic>Production management</topic><topic>Protein structure</topic><topic>Secondary structure</topic><topic>Spectroscopy</topic><topic>Stability analysis</topic><topic>Structural stability</topic><topic>Thermal stability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dastjerdeh, Mansoureh Shahbazi</creatorcontrib><creatorcontrib>Yasami-Khiabani, Setayesh</creatorcontrib><creatorcontrib>Boroujeni, Mohammadtaghi Borjian</creatorcontrib><creatorcontrib>Shokrgozar, MohammadAli</creatorcontrib><creatorcontrib>Aliabadi, Hooman 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The present study aimed to reduce aggregation propensity of rhKGF by engineering the aggregation hotspots. Initially, 21 mutants were designed based on the previously-identified aggregation-prone regions (APRs) and then four of them including mutants No. 4 (L91K, I119K), 7 (V13S, L91K), 14 (L91D, I119D), and 21 (A51E) were selected based on molecular dynamics (MD) simulations for further experimental studies. The recombinantly produced rhKGF and mutants were analyzed regarding secondary structure, thermal stability, aggregation propensity, and biological activity. Far-UV CD spectroscopy showed that the mutants have similar secondary structure with rhKGF. A51E mutant showed enhanced stability and decreased monomer loss under heat stress suggesting its reduced aggregation propensity compared to rhKGF. Mutant No. 14 showed higher stability and less aggregation tendency than mutant No. 4 indicating that only mutations decreasing p
I
of rhKGF are effective in reducing its aggregation tendency. All of the mutants were at least as potent as rhKGF in stimulating proliferation of MCF-7 epithelial cells. Our results identified A51E as an equally potent, more stable, and less aggregation-prone analog of rhKGF which could be a promising alternative drug candidate for the commercially available rhKGF (Palifermin).</abstract><cop>New York</cop><pub>Springer US</pub><pmid>36683078</pmid><doi>10.1007/s10930-023-10089-6</doi><tpages>18</tpages></addata></record> |
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| subjects | Agglomeration Analysis Animal Anatomy Biochemistry Biological activity Bioorganic Chemistry Cell proliferation Chemistry Chemistry and Materials Science Drug development Epithelial cells Epithelium Fibroblast Growth Factor 7 Growth factors Health aspects Heat stress Heat tolerance Histology Humans Keratinocyte growth factor Molecular dynamics Molecular Dynamics Simulation Morphology Mutants Mutation Organic Chemistry Palifermin Production management Protein structure Secondary structure Spectroscopy Stability analysis Structural stability Thermal stability |
| title | Rational Design and Production of Bioactive Analogs of Recombinant Human Keratinocyte Growth Factor (rhKGF) with Reduced Aggregation Propensity |
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