Collagen and keratin polypeptide models for assessing the natural and artificial protein decay of organic materials
Among the materials constituting the natural and cultural heritage, organic materials of proteinaceous origin as bone (collagen), parchment and woolen textiles (keratin) are the most susceptible to damage and decay because of their exposure to air pollution, inappropriate values of ambient temperatu...
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| Veröffentlicht in: | Journal of peptide science 2016-11, Vol.22 (11-12), p.700-710 |
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| creator | Fotou, Evmorfia Sakarellos-Daitsiotis, Maria Ioakeimoglou, Eleni Tziamourani, Eleni Malea, Ekaterini Panayiaris, George Panou-Pomonis, Eugenia |
| description | Among the materials constituting the natural and cultural heritage, organic materials of proteinaceous origin as bone (collagen), parchment and woolen textiles (keratin) are the most susceptible to damage and decay because of their exposure to air pollution, inappropriate values of ambient temperature, humidity and light. Aiming at contributing to the development of a reliable and reproducible immunoassay for the evaluation of collagen and keratin decay, three polypeptide models of these proteins were designed, synthesized and studied. Polypeptide [Pro‐Ser(OBzl)‐Gly]n incorporates the typical motif Pro‐X‐Gly of collagen; polypeptide [Pro‐Cys(Acm)‐Gly]n is a model of the C‐terminal domain of type I keratin, corresponding to the repeating unit Pro‐Cys‐X of keratin, while polypeptide Ac‐YRSGGGFGYRSGGGFGYRS‐βAla‐NH2 encloses the characteristic repeating sequence GGGFGYRS of the N‐terminal part of Type II keratin. These polypeptides may be considered as simplified models that mimic fragments of collagen and keratin resulting from artificial and natural ageing or decay. It is concluded that high recognition of anti‐polypeptide antibodies, produced after immunizations, by the bone, parchment and textile samples is indicative of high deterioration, while high anti‐collagen or anti‐keratin recognition is indicative of low deterioration. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.
Binding of anti‐collagen and anti‐[Pro‐Ser(OBzl)‐Gly]nantibodies to artificially aged bone samples in more (5) and less (10) drastic conditions. High recognition of anti‐polypeptide antibodies by the samples indicates high decay, while high anti‐collagen and anti‐keratin recognition is indicative of low decay. |
| doi_str_mv | 10.1002/psc.2933 |
| format | Article |
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Binding of anti‐collagen and anti‐[Pro‐Ser(OBzl)‐Gly]nantibodies to artificially aged bone samples in more (5) and less (10) drastic conditions. High recognition of anti‐polypeptide antibodies by the samples indicates high decay, while high anti‐collagen and anti‐keratin recognition is indicative of low decay.</description><identifier>ISSN: 1075-2617</identifier><identifier>EISSN: 1099-1387</identifier><identifier>DOI: 10.1002/psc.2933</identifier><identifier>PMID: 27739236</identifier><identifier>CODEN: JPSIEI</identifier><language>eng</language><publisher>England: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Antibodies - chemistry ; Antibodies - isolation & purification ; artificial ageing ; Collagen - administration & dosage ; Collagen - chemistry ; Collagen - immunology ; collagen polypeptide model ; ELISA experiments ; Enzyme-Linked Immunosorbent Assay ; Humans ; Immunization ; keratin polypeptide models ; Keratins - administration & dosage ; Keratins - chemistry ; Keratins - immunology ; Models, Chemical ; natural ageing ; Paleontology - methods ; Peptides ; Peptides - administration & dosage ; Peptides - chemical synthesis ; Peptides - immunology ; Proteolysis ; rabbit immunization ; Rabbits ; Time Factors</subject><ispartof>Journal of peptide science, 2016-11, Vol.22 (11-12), p.700-710</ispartof><rights>Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27739236$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fotou, Evmorfia</creatorcontrib><creatorcontrib>Sakarellos-Daitsiotis, Maria</creatorcontrib><creatorcontrib>Ioakeimoglou, Eleni</creatorcontrib><creatorcontrib>Tziamourani, Eleni</creatorcontrib><creatorcontrib>Malea, Ekaterini</creatorcontrib><creatorcontrib>Panayiaris, George</creatorcontrib><creatorcontrib>Panou-Pomonis, Eugenia</creatorcontrib><title>Collagen and keratin polypeptide models for assessing the natural and artificial protein decay of organic materials</title><title>Journal of peptide science</title><addtitle>J. Pept. Sci</addtitle><description>Among the materials constituting the natural and cultural heritage, organic materials of proteinaceous origin as bone (collagen), parchment and woolen textiles (keratin) are the most susceptible to damage and decay because of their exposure to air pollution, inappropriate values of ambient temperature, humidity and light. Aiming at contributing to the development of a reliable and reproducible immunoassay for the evaluation of collagen and keratin decay, three polypeptide models of these proteins were designed, synthesized and studied. Polypeptide [Pro‐Ser(OBzl)‐Gly]n incorporates the typical motif Pro‐X‐Gly of collagen; polypeptide [Pro‐Cys(Acm)‐Gly]n is a model of the C‐terminal domain of type I keratin, corresponding to the repeating unit Pro‐Cys‐X of keratin, while polypeptide Ac‐YRSGGGFGYRSGGGFGYRS‐βAla‐NH2 encloses the characteristic repeating sequence GGGFGYRS of the N‐terminal part of Type II keratin. These polypeptides may be considered as simplified models that mimic fragments of collagen and keratin resulting from artificial and natural ageing or decay. It is concluded that high recognition of anti‐polypeptide antibodies, produced after immunizations, by the bone, parchment and textile samples is indicative of high deterioration, while high anti‐collagen or anti‐keratin recognition is indicative of low deterioration. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.
Binding of anti‐collagen and anti‐[Pro‐Ser(OBzl)‐Gly]nantibodies to artificially aged bone samples in more (5) and less (10) drastic conditions. High recognition of anti‐polypeptide antibodies by the samples indicates high decay, while high anti‐collagen and anti‐keratin recognition is indicative of low decay.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies - chemistry</subject><subject>Antibodies - isolation & purification</subject><subject>artificial ageing</subject><subject>Collagen - administration & dosage</subject><subject>Collagen - chemistry</subject><subject>Collagen - immunology</subject><subject>collagen polypeptide model</subject><subject>ELISA experiments</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Humans</subject><subject>Immunization</subject><subject>keratin polypeptide models</subject><subject>Keratins - administration & dosage</subject><subject>Keratins - chemistry</subject><subject>Keratins - immunology</subject><subject>Models, Chemical</subject><subject>natural ageing</subject><subject>Paleontology - methods</subject><subject>Peptides</subject><subject>Peptides - administration & dosage</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - immunology</subject><subject>Proteolysis</subject><subject>rabbit immunization</subject><subject>Rabbits</subject><subject>Time Factors</subject><issn>1075-2617</issn><issn>1099-1387</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUlvFDEQhS1ERJIBiV-ALHHh0omX9naECQxEESAWwc1yd5cHJ71hu5XMv8dDQpA4cXou1Velen4IPaXkhBLCTufUnjDD-QN0RIkxFeVaPdy_laiYpOoQHad0SUjpCfkIHTKluGFcHqG0nvrebWHEbuzwFUSXw4jnqd_NMOfQAR6mDvqE_RSxSwlSCuMW5x-AR5eX6Prfgy7m4EMbSjnHKUPZ0UHrdnjyeIpbN4YWDy5DLER6jA58EXhypyv09c3rL-u31cWHzbv1y4sq8FrzypPWG6OhY15yEMxzIYmnkktfm7p1kjfQaFNL0frWU90VR4SZjtfc-8Y3fIVe3O4tJ_1cIGU7hNRC8TvCtCRLtRBEKarJf6Bc1MTQctcKPf8HvZyWOBYjhaq1ZqwmolDP7qilGaCzcwyDizv75-cLUN0C16GH3X2fErtP1JZE7T5R-_Hzeq9_-ZAy3NzzLl5ZqbgS9tv7jX11tjlT-vu5_cR_Ac3Jomw</recordid><startdate>201611</startdate><enddate>201611</enddate><creator>Fotou, Evmorfia</creator><creator>Sakarellos-Daitsiotis, Maria</creator><creator>Ioakeimoglou, Eleni</creator><creator>Tziamourani, Eleni</creator><creator>Malea, Ekaterini</creator><creator>Panayiaris, George</creator><creator>Panou-Pomonis, Eugenia</creator><general>Blackwell Publishing Ltd</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QO</scope><scope>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope><scope>7X8</scope><scope>7TV</scope><scope>C1K</scope></search><sort><creationdate>201611</creationdate><title>Collagen and keratin polypeptide models for assessing the natural and artificial protein decay of organic materials</title><author>Fotou, Evmorfia ; Sakarellos-Daitsiotis, Maria ; Ioakeimoglou, Eleni ; Tziamourani, Eleni ; Malea, Ekaterini ; Panayiaris, George ; Panou-Pomonis, Eugenia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i3483-f0cf998ed2f63e52f3560f1636f494ca63beb89465cfcf18d923029d343ffbfb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies - chemistry</topic><topic>Antibodies - isolation & purification</topic><topic>artificial ageing</topic><topic>Collagen - administration & dosage</topic><topic>Collagen - chemistry</topic><topic>Collagen - immunology</topic><topic>collagen polypeptide model</topic><topic>ELISA experiments</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Humans</topic><topic>Immunization</topic><topic>keratin polypeptide models</topic><topic>Keratins - administration & dosage</topic><topic>Keratins - chemistry</topic><topic>Keratins - immunology</topic><topic>Models, Chemical</topic><topic>natural ageing</topic><topic>Paleontology - methods</topic><topic>Peptides</topic><topic>Peptides - administration & dosage</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - immunology</topic><topic>Proteolysis</topic><topic>rabbit immunization</topic><topic>Rabbits</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fotou, Evmorfia</creatorcontrib><creatorcontrib>Sakarellos-Daitsiotis, Maria</creatorcontrib><creatorcontrib>Ioakeimoglou, Eleni</creatorcontrib><creatorcontrib>Tziamourani, Eleni</creatorcontrib><creatorcontrib>Malea, Ekaterini</creatorcontrib><creatorcontrib>Panayiaris, George</creatorcontrib><creatorcontrib>Panou-Pomonis, Eugenia</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Biotechnology Research Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Pollution Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Journal of peptide science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fotou, Evmorfia</au><au>Sakarellos-Daitsiotis, Maria</au><au>Ioakeimoglou, Eleni</au><au>Tziamourani, Eleni</au><au>Malea, Ekaterini</au><au>Panayiaris, George</au><au>Panou-Pomonis, Eugenia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Collagen and keratin polypeptide models for assessing the natural and artificial protein decay of organic materials</atitle><jtitle>Journal of peptide science</jtitle><addtitle>J. Pept. Sci</addtitle><date>2016-11</date><risdate>2016</risdate><volume>22</volume><issue>11-12</issue><spage>700</spage><epage>710</epage><pages>700-710</pages><issn>1075-2617</issn><eissn>1099-1387</eissn><coden>JPSIEI</coden><abstract>Among the materials constituting the natural and cultural heritage, organic materials of proteinaceous origin as bone (collagen), parchment and woolen textiles (keratin) are the most susceptible to damage and decay because of their exposure to air pollution, inappropriate values of ambient temperature, humidity and light. Aiming at contributing to the development of a reliable and reproducible immunoassay for the evaluation of collagen and keratin decay, three polypeptide models of these proteins were designed, synthesized and studied. Polypeptide [Pro‐Ser(OBzl)‐Gly]n incorporates the typical motif Pro‐X‐Gly of collagen; polypeptide [Pro‐Cys(Acm)‐Gly]n is a model of the C‐terminal domain of type I keratin, corresponding to the repeating unit Pro‐Cys‐X of keratin, while polypeptide Ac‐YRSGGGFGYRSGGGFGYRS‐βAla‐NH2 encloses the characteristic repeating sequence GGGFGYRS of the N‐terminal part of Type II keratin. These polypeptides may be considered as simplified models that mimic fragments of collagen and keratin resulting from artificial and natural ageing or decay. It is concluded that high recognition of anti‐polypeptide antibodies, produced after immunizations, by the bone, parchment and textile samples is indicative of high deterioration, while high anti‐collagen or anti‐keratin recognition is indicative of low deterioration. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.
Binding of anti‐collagen and anti‐[Pro‐Ser(OBzl)‐Gly]nantibodies to artificially aged bone samples in more (5) and less (10) drastic conditions. High recognition of anti‐polypeptide antibodies by the samples indicates high decay, while high anti‐collagen and anti‐keratin recognition is indicative of low decay.</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>27739236</pmid><doi>10.1002/psc.2933</doi><tpages>11</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animals Antibodies - chemistry Antibodies - isolation & purification artificial ageing Collagen - administration & dosage Collagen - chemistry Collagen - immunology collagen polypeptide model ELISA experiments Enzyme-Linked Immunosorbent Assay Humans Immunization keratin polypeptide models Keratins - administration & dosage Keratins - chemistry Keratins - immunology Models, Chemical natural ageing Paleontology - methods Peptides Peptides - administration & dosage Peptides - chemical synthesis Peptides - immunology Proteolysis rabbit immunization Rabbits Time Factors |
| title | Collagen and keratin polypeptide models for assessing the natural and artificial protein decay of organic materials |
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