Direct Observation of Phenylalanine Orientations in Statherin Bound to Hydroxyapatite Surfaces
Extracellular biomineralization proteins such as salivary statherin control the growth of hydroxyapatite (HAP), the principal component of teeth and bones. Despite the important role that statherin plays in the regulation of hard tissue formation in humans, the surface recognition mechanisms involve...
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| Veröffentlicht in: | Journal of the American Chemical Society 2012-05, Vol.134 (21), p.8750-8753 |
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| container_title | Journal of the American Chemical Society |
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| creator | Weidner, Tobias Dubey, Manish Breen, Nicholas F Ash, Jason Baio, J. E Jaye, Cherno Fischer, Daniel A Drobny, Gary P Castner, David G |
| description | Extracellular biomineralization proteins such as salivary statherin control the growth of hydroxyapatite (HAP), the principal component of teeth and bones. Despite the important role that statherin plays in the regulation of hard tissue formation in humans, the surface recognition mechanisms involved are poorly understood. The protein–surface interaction likely involves very specific contacts between the surface atoms and the key protein side chains. This study demonstrates for the first time the power of combining near-edge X-ray absorption fine structure (NEXAFS) spectroscopy with element labeling to quantify the orientation of individual side chains. In this work, the 15 amino acid N-terminal binding domain of statherin has been adsorbed onto HAP surfaces, and the orientations of phenylalanine rings F7 and F14 have been determined using NEXAFS analysis and fluorine labels at individual phenylalanine sites. The NEXAFS-derived phenylalanine tilt angles have been verified with sum frequency generation spectroscopy. |
| doi_str_mv | 10.1021/ja301711w |
| format | Article |
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E ; Jaye, Cherno ; Fischer, Daniel A ; Drobny, Gary P ; Castner, David G</creator><creatorcontrib>Weidner, Tobias ; Dubey, Manish ; Breen, Nicholas F ; Ash, Jason ; Baio, J. E ; Jaye, Cherno ; Fischer, Daniel A ; Drobny, Gary P ; Castner, David G ; BROOKHAVEN NATIONAL LABORATORY (BNL)</creatorcontrib><description>Extracellular biomineralization proteins such as salivary statherin control the growth of hydroxyapatite (HAP), the principal component of teeth and bones. Despite the important role that statherin plays in the regulation of hard tissue formation in humans, the surface recognition mechanisms involved are poorly understood. The protein–surface interaction likely involves very specific contacts between the surface atoms and the key protein side chains. This study demonstrates for the first time the power of combining near-edge X-ray absorption fine structure (NEXAFS) spectroscopy with element labeling to quantify the orientation of individual side chains. In this work, the 15 amino acid N-terminal binding domain of statherin has been adsorbed onto HAP surfaces, and the orientations of phenylalanine rings F7 and F14 have been determined using NEXAFS analysis and fluorine labels at individual phenylalanine sites. The NEXAFS-derived phenylalanine tilt angles have been verified with sum frequency generation spectroscopy.</description><identifier>ISSN: 0002-7863</identifier><identifier>ISSN: 1520-5126</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja301711w</identifier><identifier>PMID: 22563672</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>absorption ; Amino Acid Sequence ; biomineralization ; bones ; Durapatite - metabolism ; fluorine ; humans ; hydroxyapatite ; Models, Molecular ; Molecular Sequence Data ; Phenylalanine ; Protein Binding ; Protein Structure, Tertiary ; proteins ; Salivary Proteins and Peptides - chemistry ; Salivary Proteins and Peptides - metabolism ; spectroscopy ; Surface Properties ; teeth ; X-radiation ; X-Ray Absorption Spectroscopy</subject><ispartof>Journal of the American Chemical Society, 2012-05, Vol.134 (21), p.8750-8753</ispartof><rights>Copyright © 2012 American Chemical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a531t-2c09a4cb687eb5002105d29896c6e83396ddc9201d62f8f75f6d9a40d8a668e3</citedby><cites>FETCH-LOGICAL-a531t-2c09a4cb687eb5002105d29896c6e83396ddc9201d62f8f75f6d9a40d8a668e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/ja301711w$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ja301711w$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,776,780,881,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22563672$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1069578$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Weidner, Tobias</creatorcontrib><creatorcontrib>Dubey, Manish</creatorcontrib><creatorcontrib>Breen, Nicholas F</creatorcontrib><creatorcontrib>Ash, Jason</creatorcontrib><creatorcontrib>Baio, J. E</creatorcontrib><creatorcontrib>Jaye, Cherno</creatorcontrib><creatorcontrib>Fischer, Daniel A</creatorcontrib><creatorcontrib>Drobny, Gary P</creatorcontrib><creatorcontrib>Castner, David G</creatorcontrib><creatorcontrib>BROOKHAVEN NATIONAL LABORATORY (BNL)</creatorcontrib><title>Direct Observation of Phenylalanine Orientations in Statherin Bound to Hydroxyapatite Surfaces</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>Extracellular biomineralization proteins such as salivary statherin control the growth of hydroxyapatite (HAP), the principal component of teeth and bones. Despite the important role that statherin plays in the regulation of hard tissue formation in humans, the surface recognition mechanisms involved are poorly understood. The protein–surface interaction likely involves very specific contacts between the surface atoms and the key protein side chains. This study demonstrates for the first time the power of combining near-edge X-ray absorption fine structure (NEXAFS) spectroscopy with element labeling to quantify the orientation of individual side chains. In this work, the 15 amino acid N-terminal binding domain of statherin has been adsorbed onto HAP surfaces, and the orientations of phenylalanine rings F7 and F14 have been determined using NEXAFS analysis and fluorine labels at individual phenylalanine sites. The NEXAFS-derived phenylalanine tilt angles have been verified with sum frequency generation spectroscopy.</description><subject>absorption</subject><subject>Amino Acid Sequence</subject><subject>biomineralization</subject><subject>bones</subject><subject>Durapatite - metabolism</subject><subject>fluorine</subject><subject>humans</subject><subject>hydroxyapatite</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Phenylalanine</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>proteins</subject><subject>Salivary Proteins and Peptides - chemistry</subject><subject>Salivary Proteins and Peptides - metabolism</subject><subject>spectroscopy</subject><subject>Surface Properties</subject><subject>teeth</subject><subject>X-radiation</subject><subject>X-Ray Absorption Spectroscopy</subject><issn>0002-7863</issn><issn>1520-5126</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU9vEzEQxS1ERUPhwBdAFhISHBY8duz1XpCg_GmlSkFqz1iO7SWONnawdwv59kybEhWJAyePNT8_z7xHyDNgb4BxeLu2gkEL8PMBmYHkrJHA1UMyY4zxptVKHJPHta7xOucaHpFjzqUSquUz8u1jLMGNdLGsoVzbMeZEc0-_rkLaDXawKaZAFyWGNN42K42JXmK9CgWrD3lKno6Znu18yb92dovUGOjlVHrrQn1Cjno71PD07jwhV58_XZ2eNReLL-en7y8aKwWMDXess3O3VLoNS4lTA5Oed7pTTgUtRKe8dx1n4BXvdd_KXnl8wLy2SukgTsi7vex2Wm6CdzhtsYPZlrixZWeyjebvToor8z1fGyHnnQSNAi_2ArmO0VSHO7iVyymhNwaY6mR7A726-6XkH1Ooo9nE6sKALoU8VcPRYKEB_gMFzKvTmIdE9PUedSXXWkJ_GBuYuYnXHOJF9vn9PQ_knzwReLkHrKtmnaeS0PV_CP0Gv4ispg</recordid><startdate>20120530</startdate><enddate>20120530</enddate><creator>Weidner, Tobias</creator><creator>Dubey, Manish</creator><creator>Breen, Nicholas F</creator><creator>Ash, Jason</creator><creator>Baio, J. 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| source | ACS Publications; MEDLINE |
| subjects | absorption Amino Acid Sequence biomineralization bones Durapatite - metabolism fluorine humans hydroxyapatite Models, Molecular Molecular Sequence Data Phenylalanine Protein Binding Protein Structure, Tertiary proteins Salivary Proteins and Peptides - chemistry Salivary Proteins and Peptides - metabolism spectroscopy Surface Properties teeth X-radiation X-Ray Absorption Spectroscopy |
| title | Direct Observation of Phenylalanine Orientations in Statherin Bound to Hydroxyapatite Surfaces |
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