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Interaction of amelogenin with hydroxyapatite crystals: An adherence effect through amelogenin molecular self-association
At the secretory stage of tooth enamel formation the majority of the organic matrix is composed of amelogenin proteins that are believed to provide the scaffolding for the initial carbonated hydroxyapatite crystals to grow. The primary objective of this study was to investigate the interaction betwe...
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Published in: | Biopolymers 1998-10, Vol.46 (4), p.225-238 |
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description | At the secretory stage of tooth enamel formation the majority of the organic matrix is composed of amelogenin proteins that are believed to provide the scaffolding for the initial carbonated hydroxyapatite crystals to grow. The primary objective of this study was to investigate the interaction between amelogenins and growing apatite crystals. Two in vitro strategies were used: first, we examined the influence of amelogenins as compared to two other macromolecules, on the kinetics of seeded growth of apatite crystals; second, using transmission electron micrographs of the crystal powders, based on a particle size distribution study, we evaluated the effect of the macromolecules on the aggregation of growing apatite crystals. Two recombinant amelogenins (rM179, rM166), the synthetic leucine‐rich amelogenin polypeptide (LRAP), poly(L‐proline), and phosvitin were used. It was shown that the rM179 amelogenin had some inhibitory effect on the kinetics of calcium hydroxyapatite seeded growth. The inhibitory effect, however, was not as destructive as that of other macromolecules tested. The degree of inhibition of the macromolecules was in the order of phosvitin < LRAP < poly(L‐proline) < rM179 < rM166. Analysis of particle size distribution of apatite crystal aggregates indicated that the full‐length amelogenin protein (rM179) caused aggregation of the growing apatite crystals more effectively than other macromolecules. We propose that during the formation of hydroxyapatite crystal clusters, the growing apatite crystals adhere to each other through the molecular self‐association of interacting amelogenin molecules. The biological implications of this adherence effect with respect to enamel biomineralization are discussed. © 1998 John Wiley & Sons, Inc. Biopoly 46: 225–238, 1998 |
doi_str_mv | 10.1002/(SICI)1097-0282(19981005)46:4<225::AID-BIP4>3.0.CO;2-R |
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G.</creator><creatorcontrib>Moradian-Oldak, J. ; Tan, J. ; Fincham, A. G.</creatorcontrib><description>At the secretory stage of tooth enamel formation the majority of the organic matrix is composed of amelogenin proteins that are believed to provide the scaffolding for the initial carbonated hydroxyapatite crystals to grow. The primary objective of this study was to investigate the interaction between amelogenins and growing apatite crystals. Two in vitro strategies were used: first, we examined the influence of amelogenins as compared to two other macromolecules, on the kinetics of seeded growth of apatite crystals; second, using transmission electron micrographs of the crystal powders, based on a particle size distribution study, we evaluated the effect of the macromolecules on the aggregation of growing apatite crystals. Two recombinant amelogenins (rM179, rM166), the synthetic leucine‐rich amelogenin polypeptide (LRAP), poly(L‐proline), and phosvitin were used. It was shown that the rM179 amelogenin had some inhibitory effect on the kinetics of calcium hydroxyapatite seeded growth. The inhibitory effect, however, was not as destructive as that of other macromolecules tested. The degree of inhibition of the macromolecules was in the order of phosvitin < LRAP < poly(L‐proline) < rM179 < rM166. Analysis of particle size distribution of apatite crystal aggregates indicated that the full‐length amelogenin protein (rM179) caused aggregation of the growing apatite crystals more effectively than other macromolecules. We propose that during the formation of hydroxyapatite crystal clusters, the growing apatite crystals adhere to each other through the molecular self‐association of interacting amelogenin molecules. The biological implications of this adherence effect with respect to enamel biomineralization are discussed. © 1998 John Wiley & Sons, Inc. Biopoly 46: 225–238, 1998</description><identifier>ISSN: 0006-3525</identifier><identifier>EISSN: 1097-0282</identifier><identifier>DOI: 10.1002/(SICI)1097-0282(19981005)46:4<225::AID-BIP4>3.0.CO;2-R</identifier><identifier>PMID: 9715666</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Amelogenin ; Amino Acids - analysis ; apatite ; crystal growth ; Crystallization ; Dental Enamel Proteins - chemistry ; Hydroxyapatites - chemistry ; Microscopy, Electron ; molecular self-association ; Peptides - chemistry ; Phosvitin - chemistry ; Recombinant Proteins - chemistry ; Structure-Activity Relationship ; Surface Properties ; tooth enamel ; Tooth Germ - chemistry</subject><ispartof>Biopolymers, 1998-10, Vol.46 (4), p.225-238</ispartof><rights>Copyright © 1998 John Wiley & Sons, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c4024-ee3052c1288ae87750970db054a3990d3f9de3735c38c873277998a31193c2943</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9715666$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Moradian-Oldak, J.</creatorcontrib><creatorcontrib>Tan, J.</creatorcontrib><creatorcontrib>Fincham, A. G.</creatorcontrib><title>Interaction of amelogenin with hydroxyapatite crystals: An adherence effect through amelogenin molecular self-association</title><title>Biopolymers</title><addtitle>Biopolymers</addtitle><description>At the secretory stage of tooth enamel formation the majority of the organic matrix is composed of amelogenin proteins that are believed to provide the scaffolding for the initial carbonated hydroxyapatite crystals to grow. The primary objective of this study was to investigate the interaction between amelogenins and growing apatite crystals. Two in vitro strategies were used: first, we examined the influence of amelogenins as compared to two other macromolecules, on the kinetics of seeded growth of apatite crystals; second, using transmission electron micrographs of the crystal powders, based on a particle size distribution study, we evaluated the effect of the macromolecules on the aggregation of growing apatite crystals. Two recombinant amelogenins (rM179, rM166), the synthetic leucine‐rich amelogenin polypeptide (LRAP), poly(L‐proline), and phosvitin were used. It was shown that the rM179 amelogenin had some inhibitory effect on the kinetics of calcium hydroxyapatite seeded growth. The inhibitory effect, however, was not as destructive as that of other macromolecules tested. The degree of inhibition of the macromolecules was in the order of phosvitin < LRAP < poly(L‐proline) < rM179 < rM166. Analysis of particle size distribution of apatite crystal aggregates indicated that the full‐length amelogenin protein (rM179) caused aggregation of the growing apatite crystals more effectively than other macromolecules. We propose that during the formation of hydroxyapatite crystal clusters, the growing apatite crystals adhere to each other through the molecular self‐association of interacting amelogenin molecules. The biological implications of this adherence effect with respect to enamel biomineralization are discussed. © 1998 John Wiley & Sons, Inc. Biopoly 46: 225–238, 1998</description><subject>Amelogenin</subject><subject>Amino Acids - analysis</subject><subject>apatite</subject><subject>crystal growth</subject><subject>Crystallization</subject><subject>Dental Enamel Proteins - chemistry</subject><subject>Hydroxyapatites - chemistry</subject><subject>Microscopy, Electron</subject><subject>molecular self-association</subject><subject>Peptides - chemistry</subject><subject>Phosvitin - chemistry</subject><subject>Recombinant Proteins - chemistry</subject><subject>Structure-Activity Relationship</subject><subject>Surface Properties</subject><subject>tooth enamel</subject><subject>Tooth Germ - chemistry</subject><issn>0006-3525</issn><issn>1097-0282</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNqFkV1v0zAUhiMEGmXwE5ByhbaLlOOvOCloUgkwIlUUjQGXR55zsoalSbFTbfn3JGspSCBxZVk-fl77fYLgjMGUAfCXJ5_zLD9lkOoIeMJPWJomw4E6lfFMvuZczWbz_G30Jv8kz8QUptnyFY8uHgSTw5WHwQQA4kgorh4HT7z_DiClYHAUHKWaqTiOJ0GfNx05Y7uqbcK2DM2a6vaamqoJb6tuFa76wrV3vdmYruootK73nan9LJw3oSlW5KixFFJZku3CbuXa7fXqT8i6rclua-NCT3UZGe9bW5kx7WnwqBxI9Gy_Hgdf3r-7zD5Ei-V5ns0XkZXAZUQkQHHLeJIYSrRWw_eguAIljUhTKESZFiS0UFYkNtGCaz00ZQRjqbA8leI4eLHjblz7Y0u-w3XlLdW1aajdetQiiUHfD37dDVrXeu-oxI2r1sb1yABHJ4ijExwLxrFg_OUEZYwSByeIgxMcnaBAwGyJHC8G8PP9C7ZXayoO2L2E38G3VU39X6n_Df1H5v1-AEc7cOU7ujuAjbvBWAut8NvHc-TJgkGiLjETPwHJurcn</recordid><startdate>19981005</startdate><enddate>19981005</enddate><creator>Moradian-Oldak, J.</creator><creator>Tan, J.</creator><creator>Fincham, A. G.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</scope><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></search><sort><creationdate>19981005</creationdate><title>Interaction of amelogenin with hydroxyapatite crystals: An adherence effect through amelogenin molecular self-association</title><author>Moradian-Oldak, J. ; Tan, J. ; Fincham, A. G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4024-ee3052c1288ae87750970db054a3990d3f9de3735c38c873277998a31193c2943</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amelogenin</topic><topic>Amino Acids - analysis</topic><topic>apatite</topic><topic>crystal growth</topic><topic>Crystallization</topic><topic>Dental Enamel Proteins - chemistry</topic><topic>Hydroxyapatites - chemistry</topic><topic>Microscopy, Electron</topic><topic>molecular self-association</topic><topic>Peptides - chemistry</topic><topic>Phosvitin - chemistry</topic><topic>Recombinant Proteins - chemistry</topic><topic>Structure-Activity Relationship</topic><topic>Surface Properties</topic><topic>tooth enamel</topic><topic>Tooth Germ - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moradian-Oldak, J.</creatorcontrib><creatorcontrib>Tan, J.</creatorcontrib><creatorcontrib>Fincham, A. G.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biopolymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moradian-Oldak, J.</au><au>Tan, J.</au><au>Fincham, A. G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of amelogenin with hydroxyapatite crystals: An adherence effect through amelogenin molecular self-association</atitle><jtitle>Biopolymers</jtitle><addtitle>Biopolymers</addtitle><date>1998-10-05</date><risdate>1998</risdate><volume>46</volume><issue>4</issue><spage>225</spage><epage>238</epage><pages>225-238</pages><issn>0006-3525</issn><eissn>1097-0282</eissn><abstract>At the secretory stage of tooth enamel formation the majority of the organic matrix is composed of amelogenin proteins that are believed to provide the scaffolding for the initial carbonated hydroxyapatite crystals to grow. The primary objective of this study was to investigate the interaction between amelogenins and growing apatite crystals. Two in vitro strategies were used: first, we examined the influence of amelogenins as compared to two other macromolecules, on the kinetics of seeded growth of apatite crystals; second, using transmission electron micrographs of the crystal powders, based on a particle size distribution study, we evaluated the effect of the macromolecules on the aggregation of growing apatite crystals. Two recombinant amelogenins (rM179, rM166), the synthetic leucine‐rich amelogenin polypeptide (LRAP), poly(L‐proline), and phosvitin were used. It was shown that the rM179 amelogenin had some inhibitory effect on the kinetics of calcium hydroxyapatite seeded growth. The inhibitory effect, however, was not as destructive as that of other macromolecules tested. The degree of inhibition of the macromolecules was in the order of phosvitin < LRAP < poly(L‐proline) < rM179 < rM166. Analysis of particle size distribution of apatite crystal aggregates indicated that the full‐length amelogenin protein (rM179) caused aggregation of the growing apatite crystals more effectively than other macromolecules. We propose that during the formation of hydroxyapatite crystal clusters, the growing apatite crystals adhere to each other through the molecular self‐association of interacting amelogenin molecules. The biological implications of this adherence effect with respect to enamel biomineralization are discussed. © 1998 John Wiley & Sons, Inc. Biopoly 46: 225–238, 1998</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>9715666</pmid><doi>10.1002/(SICI)1097-0282(19981005)46:4<225::AID-BIP4>3.0.CO;2-R</doi><tpages>14</tpages></addata></record> |
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subjects | Amelogenin Amino Acids - analysis apatite crystal growth Crystallization Dental Enamel Proteins - chemistry Hydroxyapatites - chemistry Microscopy, Electron molecular self-association Peptides - chemistry Phosvitin - chemistry Recombinant Proteins - chemistry Structure-Activity Relationship Surface Properties tooth enamel Tooth Germ - chemistry |
title | Interaction of amelogenin with hydroxyapatite crystals: An adherence effect through amelogenin molecular self-association |
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