Collagen Glycation Detected by Its Intrinsic Fluorescence
Collagen’s long half-life (in skin approximately 10 years) makes this protein highly susceptible to glycation and formation of the advanced glycation end products (AGEs). Accumulation of cross-linking AGEs in the skin collagen has several detrimental effects; thus, the opportunity for non-invasive m...
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| Veröffentlicht in: | The journal of physical chemistry. B 2021-10, Vol.125 (39), p.11058-11066 |
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| container_end_page | 11066 |
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| container_issue | 39 |
| container_start_page | 11058 |
| container_title | The journal of physical chemistry. B |
| container_volume | 125 |
| creator | Muir, Rhona Forbes, Shareen Birch, David J.S Vyshemirsky, Vladislav Rolinski, Olaf J |
| description | Collagen’s long half-life (in skin approximately 10 years) makes this protein highly susceptible to glycation and formation of the advanced glycation end products (AGEs). Accumulation of cross-linking AGEs in the skin collagen has several detrimental effects; thus, the opportunity for non-invasive monitoring of skin glycation is essential, especially for diabetic patients. In this paper, we report using the time-resolved intrinsic fluorescence of collagen as a biomarker of its glycation. Contrary to the traditional fluorescence intensity decay measurement at the arbitrarily selected excitation and detection wavelengths, we conducted systematic wavelength- and time-resolved measurements to achieve time-resolved emission spectra. Changes in the intrinsic fluorescence kinetics, caused by both collagen aggregation and glycation, have been detected. |
| doi_str_mv | 10.1021/acs.jpcb.1c05001 |
| format | Article |
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Accumulation of cross-linking AGEs in the skin collagen has several detrimental effects; thus, the opportunity for non-invasive monitoring of skin glycation is essential, especially for diabetic patients. In this paper, we report using the time-resolved intrinsic fluorescence of collagen as a biomarker of its glycation. Contrary to the traditional fluorescence intensity decay measurement at the arbitrarily selected excitation and detection wavelengths, we conducted systematic wavelength- and time-resolved measurements to achieve time-resolved emission spectra. 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Changes in the intrinsic fluorescence kinetics, caused by both collagen aggregation and glycation, have been detected.</description><subject>B: Soft Matter, Fluid Interfaces, Colloids, Polymers, and Glassy Materials</subject><subject>Collagen</subject><subject>Fluorescence</subject><subject>Glycation End Products, Advanced</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Skin</subject><issn>1520-6106</issn><issn>1520-5207</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kDFPwzAQhS0EolDYmVBGBlLOdu3ECxIqtFSqxAKz5ThOSZXGxXaQ-u9xaahgYDj5JL_37u5D6ArDCAPBd0r70WqjixHWwADwETrDjEAaKzvue46BD9C59ysAwkjOT9GAjhljAugZEhPbNGpp2mTWbLUKtW2TRxOMDqZMim0yDz6Zt8HVra91Mm0664zXptXmAp1UqvHmsn-H6G369Dp5Thcvs_nkYZGqMaUhJUKA4JoanClKSkFyyEoQ1GidFblQJCsrwaFgphB5CRUZ8wqzQuisKkVFgQ7R_T530xVrU8bZwalGbly9Vm4rrarl35-2fpdL-ynzTFBM8xhw0wc4-9EZH-S6jifEs1tjOy8JyzhnPB-TKIW9VDvrvTPVYQwGuSMuI3G5Iy574tFy_Xu9g-EHcRTc7gXfVtu5NtL6P-8LJpKNHQ</recordid><startdate>20211007</startdate><enddate>20211007</enddate><creator>Muir, Rhona</creator><creator>Forbes, Shareen</creator><creator>Birch, David J.S</creator><creator>Vyshemirsky, Vladislav</creator><creator>Rolinski, Olaf J</creator><general>American Chemical Society</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>5PM</scope><orcidid>https://orcid.org/0000-0002-7838-779X</orcidid></search><sort><creationdate>20211007</creationdate><title>Collagen Glycation Detected by Its Intrinsic Fluorescence</title><author>Muir, Rhona ; Forbes, Shareen ; Birch, David J.S ; Vyshemirsky, Vladislav ; Rolinski, Olaf J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a433t-299096c3e17a32d92807d093ecc7b89a27df960b5eb98d0f246f15b9c7fd9f303</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>B: Soft Matter, Fluid Interfaces, Colloids, Polymers, and Glassy Materials</topic><topic>Collagen</topic><topic>Fluorescence</topic><topic>Glycation End Products, Advanced</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Skin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Muir, Rhona</creatorcontrib><creatorcontrib>Forbes, Shareen</creatorcontrib><creatorcontrib>Birch, David J.S</creatorcontrib><creatorcontrib>Vyshemirsky, Vladislav</creatorcontrib><creatorcontrib>Rolinski, Olaf J</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>The journal of physical chemistry. 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| source | MEDLINE; American Chemical Society Journals |
| subjects | B: Soft Matter, Fluid Interfaces, Colloids, Polymers, and Glassy Materials Collagen Fluorescence Glycation End Products, Advanced Humans Kinetics Skin |
| title | Collagen Glycation Detected by Its Intrinsic Fluorescence |
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