Alginate as an antiglycating agent for human serum albumin
Hyperglycemia and the accumulation of advanced glycation endproducts (AGEs) in tissues and serum have important roles in diabetic complications. Therefore, the identification of anti-glycation compounds is attracting considerable interest. In this study, the interaction of human serum albumin (HSA)...
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| Veröffentlicht in: | International journal of biological macromolecules 2007-07, Vol.41 (2), p.180-184 |
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| container_title | International journal of biological macromolecules |
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| creator | Sattarahmady, Naghmeh Khodagholi, Fariba Moosavi-Movahedi, Ali A. Heli, Hossein Hakimelahi, Gholam H. |
| description | Hyperglycemia and the accumulation of advanced glycation endproducts (AGEs) in tissues and serum have important roles in diabetic complications. Therefore, the identification of anti-glycation compounds is attracting considerable interest.
In this study, the interaction of human serum albumin (HSA) with fructose, in the absence and presence of alginate, was studied by circular dichroism, absorbance and fluorescence techniques. The characterization study of AGEs was performed using autofluorescence, fibrillar formation, the increase in absorbance and the quantification of free lysine side chains. The results indicate that alginate inhibits the fructation of HSA as observed by a reduction in the formation of fluorescent AGEs and fibrils. Furthermore, alginate reduces the amount of modified lysine side chains, signified by the lack of increase in absorbance, and increases the helicity of this protein. |
| doi_str_mv | 10.1016/j.ijbiomac.2007.01.015 |
| format | Article |
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In this study, the interaction of human serum albumin (HSA) with fructose, in the absence and presence of alginate, was studied by circular dichroism, absorbance and fluorescence techniques. The characterization study of AGEs was performed using autofluorescence, fibrillar formation, the increase in absorbance and the quantification of free lysine side chains. The results indicate that alginate inhibits the fructation of HSA as observed by a reduction in the formation of fluorescent AGEs and fibrils. Furthermore, alginate reduces the amount of modified lysine side chains, signified by the lack of increase in absorbance, and increases the helicity of this protein.</description><identifier>ISSN: 0141-8130</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2007.01.015</identifier><identifier>PMID: 17350677</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Alginate ; Alginates - chemistry ; Anti-AGE ; Diabetic disease ; Fructose ; Fructose - chemistry ; Glucuronic Acid - chemistry ; Glycation ; Glycation End Products, Advanced - chemistry ; Glycation End Products, Advanced - metabolism ; Glycosylation ; Hexuronic Acids - chemistry ; HSA ; Humans ; Hyperglycemia - metabolism ; Lysine - chemistry ; Lysine - metabolism ; Protein Structure, Secondary ; Serum Albumin - chemistry ; Serum Albumin - metabolism ; Spectrum Analysis</subject><ispartof>International journal of biological macromolecules, 2007-07, Vol.41 (2), p.180-184</ispartof><rights>2007 Elsevier B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c366t-962cc9f6310677a0e0a9d259dbc2ec234d6f209d591fc09a362da94871df69543</citedby><cites>FETCH-LOGICAL-c366t-962cc9f6310677a0e0a9d259dbc2ec234d6f209d591fc09a362da94871df69543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0141813007000499$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17350677$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sattarahmady, Naghmeh</creatorcontrib><creatorcontrib>Khodagholi, Fariba</creatorcontrib><creatorcontrib>Moosavi-Movahedi, Ali A.</creatorcontrib><creatorcontrib>Heli, Hossein</creatorcontrib><creatorcontrib>Hakimelahi, Gholam H.</creatorcontrib><title>Alginate as an antiglycating agent for human serum albumin</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>Hyperglycemia and the accumulation of advanced glycation endproducts (AGEs) in tissues and serum have important roles in diabetic complications. Therefore, the identification of anti-glycation compounds is attracting considerable interest.
In this study, the interaction of human serum albumin (HSA) with fructose, in the absence and presence of alginate, was studied by circular dichroism, absorbance and fluorescence techniques. The characterization study of AGEs was performed using autofluorescence, fibrillar formation, the increase in absorbance and the quantification of free lysine side chains. The results indicate that alginate inhibits the fructation of HSA as observed by a reduction in the formation of fluorescent AGEs and fibrils. Furthermore, alginate reduces the amount of modified lysine side chains, signified by the lack of increase in absorbance, and increases the helicity of this protein.</description><subject>Alginate</subject><subject>Alginates - chemistry</subject><subject>Anti-AGE</subject><subject>Diabetic disease</subject><subject>Fructose</subject><subject>Fructose - chemistry</subject><subject>Glucuronic Acid - chemistry</subject><subject>Glycation</subject><subject>Glycation End Products, Advanced - chemistry</subject><subject>Glycation End Products, Advanced - metabolism</subject><subject>Glycosylation</subject><subject>Hexuronic Acids - chemistry</subject><subject>HSA</subject><subject>Humans</subject><subject>Hyperglycemia - metabolism</subject><subject>Lysine - chemistry</subject><subject>Lysine - metabolism</subject><subject>Protein Structure, Secondary</subject><subject>Serum Albumin - chemistry</subject><subject>Serum Albumin - metabolism</subject><subject>Spectrum Analysis</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUMtqwzAQFKWlSdP-QvCpN6cry5atnhpCXxDopT0LWVq7Mn6kkl3I31chKT0WBhZ2Z3aYIWRJYUWB8rtmZZvSDp3SqwQgXwENyM7InBa5iAGAnZM50JTGBWUwI1feN2HLM1pckhnNWQY8z-fkft3WtlcjRspHqg8Ybd3utRptX0eqxn6MqsFFn1MXrh7d1EWqLafO9tfkolKtx5vTXJCPp8f3zUu8fXt-3ay3sWacj7Hgidai4oweHBUgKGGSTJhSJ6gTlhpeJSBMJmilQSjGE6NEWuTUVFxkKVuQ2-PfnRu-JvSj7KzX2Laqx2HyMoc0hSIkXhB-JGo3eO-wkjtnO-X2koI8tCYb-duaPLQmgQZkQbg8OUxlh-ZPdqopEB6OBAw5vy066bXFXqOxDvUozWD_8_gB64WARQ</recordid><startdate>20070701</startdate><enddate>20070701</enddate><creator>Sattarahmady, Naghmeh</creator><creator>Khodagholi, Fariba</creator><creator>Moosavi-Movahedi, Ali A.</creator><creator>Heli, Hossein</creator><creator>Hakimelahi, Gholam H.</creator><general>Elsevier B.V</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></search><sort><creationdate>20070701</creationdate><title>Alginate as an antiglycating agent for human serum albumin</title><author>Sattarahmady, Naghmeh ; Khodagholi, Fariba ; Moosavi-Movahedi, Ali A. ; Heli, Hossein ; Hakimelahi, Gholam H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c366t-962cc9f6310677a0e0a9d259dbc2ec234d6f209d591fc09a362da94871df69543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Alginate</topic><topic>Alginates - chemistry</topic><topic>Anti-AGE</topic><topic>Diabetic disease</topic><topic>Fructose</topic><topic>Fructose - chemistry</topic><topic>Glucuronic Acid - chemistry</topic><topic>Glycation</topic><topic>Glycation End Products, Advanced - chemistry</topic><topic>Glycation End Products, Advanced - metabolism</topic><topic>Glycosylation</topic><topic>Hexuronic Acids - chemistry</topic><topic>HSA</topic><topic>Humans</topic><topic>Hyperglycemia - metabolism</topic><topic>Lysine - chemistry</topic><topic>Lysine - metabolism</topic><topic>Protein Structure, Secondary</topic><topic>Serum Albumin - chemistry</topic><topic>Serum Albumin - metabolism</topic><topic>Spectrum Analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sattarahmady, Naghmeh</creatorcontrib><creatorcontrib>Khodagholi, Fariba</creatorcontrib><creatorcontrib>Moosavi-Movahedi, Ali A.</creatorcontrib><creatorcontrib>Heli, Hossein</creatorcontrib><creatorcontrib>Hakimelahi, Gholam H.</creatorcontrib><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>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sattarahmady, Naghmeh</au><au>Khodagholi, Fariba</au><au>Moosavi-Movahedi, Ali A.</au><au>Heli, Hossein</au><au>Hakimelahi, Gholam H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Alginate as an antiglycating agent for human serum albumin</atitle><jtitle>International journal of biological macromolecules</jtitle><addtitle>Int J Biol Macromol</addtitle><date>2007-07-01</date><risdate>2007</risdate><volume>41</volume><issue>2</issue><spage>180</spage><epage>184</epage><pages>180-184</pages><issn>0141-8130</issn><eissn>1879-0003</eissn><abstract>Hyperglycemia and the accumulation of advanced glycation endproducts (AGEs) in tissues and serum have important roles in diabetic complications. Therefore, the identification of anti-glycation compounds is attracting considerable interest.
In this study, the interaction of human serum albumin (HSA) with fructose, in the absence and presence of alginate, was studied by circular dichroism, absorbance and fluorescence techniques. The characterization study of AGEs was performed using autofluorescence, fibrillar formation, the increase in absorbance and the quantification of free lysine side chains. The results indicate that alginate inhibits the fructation of HSA as observed by a reduction in the formation of fluorescent AGEs and fibrils. Furthermore, alginate reduces the amount of modified lysine side chains, signified by the lack of increase in absorbance, and increases the helicity of this protein.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>17350677</pmid><doi>10.1016/j.ijbiomac.2007.01.015</doi><tpages>5</tpages></addata></record> |
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| ispartof | International journal of biological macromolecules, 2007-07, Vol.41 (2), p.180-184 |
| issn | 0141-8130 1879-0003 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Alginate Alginates - chemistry Anti-AGE Diabetic disease Fructose Fructose - chemistry Glucuronic Acid - chemistry Glycation Glycation End Products, Advanced - chemistry Glycation End Products, Advanced - metabolism Glycosylation Hexuronic Acids - chemistry HSA Humans Hyperglycemia - metabolism Lysine - chemistry Lysine - metabolism Protein Structure, Secondary Serum Albumin - chemistry Serum Albumin - metabolism Spectrum Analysis |
| title | Alginate as an antiglycating agent for human serum albumin |
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