High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: implication of suppression of protein aggregation by arginine
While biotechnological applications of arginine (Arg) as a solution additive that prevents protein aggregation are increasing, the molecular mechanism of its effects remains unclear. In this study, we investigated the Arg–lysozyme complex by high-resolution crystallographic analysis. Three Arg molec...
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| Veröffentlicht in: | Protein engineering, design and selection design and selection, 2011-03, Vol.24 (3), p.269-274 |
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| container_title | Protein engineering, design and selection |
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| creator | Ito, Len Shiraki, Kentaro Matsuura, Takanori Okumura, Masaki Hasegawa, Kazuya Baba, Seiki Yamaguchi, Hiroshi Kumasaka, Takashi |
| description | While biotechnological applications of arginine (Arg) as a solution additive that prevents protein aggregation are increasing, the molecular mechanism of its effects remains unclear. In this study, we investigated the Arg–lysozyme complex by high-resolution crystallographic analysis. Three Arg molecules were observed to be in close proximity to aromatic amino acid residues of the protein surface, and their occupancies gradually increased with increasing Arg concentration. These interactions were mediated by electrostatic, hydrophobic and cation–π interactions with the surface residues. The binding of Arg decreased the accessible surface area of aromatic residues by 40%, but increased that of charged residues by 10%. These changes might prevent intermolecular hydrophobic interactions by shielding hydrophobic regions of the lysozyme surface, resulting in an increase in protein solubility. |
| doi_str_mv | 10.1093/protein/gzq101 |
| format | Article |
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In this study, we investigated the Arg–lysozyme complex by high-resolution crystallographic analysis. Three Arg molecules were observed to be in close proximity to aromatic amino acid residues of the protein surface, and their occupancies gradually increased with increasing Arg concentration. These interactions were mediated by electrostatic, hydrophobic and cation–π interactions with the surface residues. The binding of Arg decreased the accessible surface area of aromatic residues by 40%, but increased that of charged residues by 10%. These changes might prevent intermolecular hydrophobic interactions by shielding hydrophobic regions of the lysozyme surface, resulting in an increase in protein solubility.</description><identifier>ISSN: 1741-0126</identifier><identifier>EISSN: 1741-0134</identifier><identifier>DOI: 10.1093/protein/gzq101</identifier><identifier>PMID: 21084280</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Animals ; Arginine - metabolism ; Arginine - pharmacology ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Muramidase - chemistry ; Muramidase - metabolism ; Protein Binding ; Protein Multimerization - drug effects ; Protein Structure, Quaternary ; Solubility ; Spectrometry, Fluorescence</subject><ispartof>Protein engineering, design and selection, 2011-03, Vol.24 (3), p.269-274</ispartof><rights>The Author 2010. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oup.com 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c466t-88b893df3c1f60078706ee3feb62b1ecc4b75d8382e109c87ff23e743a7829843</citedby><cites>FETCH-LOGICAL-c466t-88b893df3c1f60078706ee3feb62b1ecc4b75d8382e109c87ff23e743a7829843</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1578,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21084280$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ito, Len</creatorcontrib><creatorcontrib>Shiraki, Kentaro</creatorcontrib><creatorcontrib>Matsuura, Takanori</creatorcontrib><creatorcontrib>Okumura, Masaki</creatorcontrib><creatorcontrib>Hasegawa, Kazuya</creatorcontrib><creatorcontrib>Baba, Seiki</creatorcontrib><creatorcontrib>Yamaguchi, Hiroshi</creatorcontrib><creatorcontrib>Kumasaka, Takashi</creatorcontrib><title>High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: implication of suppression of protein aggregation by arginine</title><title>Protein engineering, design and selection</title><addtitle>Protein Eng Des Sel</addtitle><description>While biotechnological applications of arginine (Arg) as a solution additive that prevents protein aggregation are increasing, the molecular mechanism of its effects remains unclear. In this study, we investigated the Arg–lysozyme complex by high-resolution crystallographic analysis. Three Arg molecules were observed to be in close proximity to aromatic amino acid residues of the protein surface, and their occupancies gradually increased with increasing Arg concentration. These interactions were mediated by electrostatic, hydrophobic and cation–π interactions with the surface residues. The binding of Arg decreased the accessible surface area of aromatic residues by 40%, but increased that of charged residues by 10%. These changes might prevent intermolecular hydrophobic interactions by shielding hydrophobic regions of the lysozyme surface, resulting in an increase in protein solubility.</description><subject>Animals</subject><subject>Arginine - metabolism</subject><subject>Arginine - pharmacology</subject><subject>Crystallography, X-Ray</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Models, Molecular</subject><subject>Muramidase - chemistry</subject><subject>Muramidase - metabolism</subject><subject>Protein Binding</subject><subject>Protein Multimerization - drug effects</subject><subject>Protein Structure, Quaternary</subject><subject>Solubility</subject><subject>Spectrometry, Fluorescence</subject><issn>1741-0126</issn><issn>1741-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9r3DAQxUVoSLZJrjkW3UoOTvTHK8m9ldB0Cwu9JJCbkeWRo2JbjmQXnI_TT1qldve66KAR_N7MPD2Erim5paTgd0PwI7j-rnl7pYSeoA2VOc0I5fmHQ83EOfoY4y9CmJCUnqFzRonKmSIb9GfnmpcsQPTtNDrf4-cs6BnrXrdzdBEH-A26jbhyfe36BnuLdWhc73rAo0-17_ToTOKiqyeI70BS-re5AxynYLWBL9h1Q-uM_jcgAXEahiSI63P1gHXTBGgWqpoPcy7RqU0rwNV6X6Cnh2-P97ts__P7j_uv-8zkQoyZUpUqeG25oVYQIpUkAoBbqASrKBiTV3JbK64YpJ8zSlrLOMica6lYoXJ-gT4vfdM-r8nKWHYuGmhb3YOfYllsc5EOk0dJtaUF54KTRN4upAk-xgC2HILrdJhLSsr3AMvVfLkEmASf1tZT1UF9wP8nloCbBfDTcKzZX_jnq98</recordid><startdate>20110301</startdate><enddate>20110301</enddate><creator>Ito, Len</creator><creator>Shiraki, Kentaro</creator><creator>Matsuura, Takanori</creator><creator>Okumura, Masaki</creator><creator>Hasegawa, Kazuya</creator><creator>Baba, Seiki</creator><creator>Yamaguchi, Hiroshi</creator><creator>Kumasaka, Takashi</creator><general>Oxford University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20110301</creationdate><title>High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: implication of suppression of protein aggregation by arginine</title><author>Ito, Len ; 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| ispartof | Protein engineering, design and selection, 2011-03, Vol.24 (3), p.269-274 |
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| source | Oxford University Press Journals; MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Animals Arginine - metabolism Arginine - pharmacology Crystallography, X-Ray Hydrophobic and Hydrophilic Interactions Models, Molecular Muramidase - chemistry Muramidase - metabolism Protein Binding Protein Multimerization - drug effects Protein Structure, Quaternary Solubility Spectrometry, Fluorescence |
| title | High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: implication of suppression of protein aggregation by arginine |
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