FTIR markers of methionine oxidation for early detection of oxidized protein therapeutics
The biological activity of therapeutic proteins is strongly dependent on the stability of their folded state, which can easily be compromised by degradation. Oxidation is one of the most common causes of degradation and is typically associated with impairment of the native protein structure. Methion...
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Veröffentlicht in: | European biophysics journal 2011-03, Vol.40 (3), p.339-345 |
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description | The biological activity of therapeutic proteins is strongly dependent on the stability of their folded state, which can easily be compromised by degradation. Oxidation is one of the most common causes of degradation and is typically associated with impairment of the native protein structure. Methionine residues stand out as particularly susceptible to oxidation by reactive oxygen intermediates even under mild conditions. Consequently, methionine oxidation has profound effects on protein activity up to the point of adverse biological responses. Of immediate importance therefore is finding affordable approaches for rapid detection of methionine oxidation before any substantial structural changes can ensue. Herein we report that vibrational bands at 1,044 and 1,113 cm
−1
in the mid-infrared region can serve as characteristic markers of methionine oxidation in oxidatively stressed protein therapeutics, monoclonal antibodies (IgG1 and its antigen-binding fragment). Such Fourier-transform infrared (FTIR) markers underpin rapid detection assays and hold particular promise for correlation of methionine oxidation with protein structure and function. |
doi_str_mv | 10.1007/s00249-010-0656-1 |
format | Article |
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−1
in the mid-infrared region can serve as characteristic markers of methionine oxidation in oxidatively stressed protein therapeutics, monoclonal antibodies (IgG1 and its antigen-binding fragment). Such Fourier-transform infrared (FTIR) markers underpin rapid detection assays and hold particular promise for correlation of methionine oxidation with protein structure and function.</description><identifier>ISSN: 0175-7571</identifier><identifier>EISSN: 1432-1017</identifier><identifier>DOI: 10.1007/s00249-010-0656-1</identifier><identifier>PMID: 21229353</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>Biochemistry ; Biodegradation ; Biological and Medical Physics ; Biomarkers - analysis ; Biomarkers - chemistry ; Biomedical and Life Sciences ; Biophysics ; Biophysics Letter ; Cell Biology ; Circular Dichroism - methods ; Fourier transforms ; Immunoglobulin Fab Fragments - analysis ; Immunoglobulin Fab Fragments - chemistry ; Immunoglobulin Fab Fragments - therapeutic use ; Immunoglobulin Fc Fragments - analysis ; Immunoglobulin Fc Fragments - chemistry ; Immunoglobulin Fc Fragments - therapeutic use ; Immunoglobulin G - analysis ; Immunoglobulin G - chemistry ; Immunoglobulin G - therapeutic use ; Life Sciences ; Membrane Biology ; Methionine - analogs & derivatives ; Methionine - analysis ; Methionine - chemistry ; Nanotechnology ; Neurobiology ; Oxidation ; Oxidation-Reduction ; Oxidative Stress ; Proteins ; Quantitative Structure-Activity Relationship ; Spectrometry, Fluorescence ; Spectroscopy, Fourier Transform Infrared ; Spectrum analysis</subject><ispartof>European biophysics journal, 2011-03, Vol.40 (3), p.339-345</ispartof><rights>Her Majesty the Queen in Right of Australia as represented by the Commonwealth Scientific and Industrial Research Organisation 2011</rights><rights>European Biophysical Societies' Association 2011</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c370t-2c1b962ff472bbd28a176feb8f4f55743686a7c7e3194e55a3393add0560a2c93</citedby><cites>FETCH-LOGICAL-c370t-2c1b962ff472bbd28a176feb8f4f55743686a7c7e3194e55a3393add0560a2c93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00249-010-0656-1$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00249-010-0656-1$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21229353$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ravi, Jascindra</creatorcontrib><creatorcontrib>Hills, Anna E.</creatorcontrib><creatorcontrib>Cerasoli, Eleonora</creatorcontrib><creatorcontrib>Rakowska, Paulina D.</creatorcontrib><creatorcontrib>Ryadnov, Maxim G.</creatorcontrib><title>FTIR markers of methionine oxidation for early detection of oxidized protein therapeutics</title><title>European biophysics journal</title><addtitle>Eur Biophys J</addtitle><addtitle>Eur Biophys J</addtitle><description>The biological activity of therapeutic proteins is strongly dependent on the stability of their folded state, which can easily be compromised by degradation. Oxidation is one of the most common causes of degradation and is typically associated with impairment of the native protein structure. Methionine residues stand out as particularly susceptible to oxidation by reactive oxygen intermediates even under mild conditions. Consequently, methionine oxidation has profound effects on protein activity up to the point of adverse biological responses. Of immediate importance therefore is finding affordable approaches for rapid detection of methionine oxidation before any substantial structural changes can ensue. Herein we report that vibrational bands at 1,044 and 1,113 cm
−1
in the mid-infrared region can serve as characteristic markers of methionine oxidation in oxidatively stressed protein therapeutics, monoclonal antibodies (IgG1 and its antigen-binding fragment). Such Fourier-transform infrared (FTIR) markers underpin rapid detection assays and hold particular promise for correlation of methionine oxidation with protein structure and function.</description><subject>Biochemistry</subject><subject>Biodegradation</subject><subject>Biological and Medical Physics</subject><subject>Biomarkers - analysis</subject><subject>Biomarkers - chemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biophysics</subject><subject>Biophysics Letter</subject><subject>Cell Biology</subject><subject>Circular Dichroism - methods</subject><subject>Fourier transforms</subject><subject>Immunoglobulin Fab Fragments - analysis</subject><subject>Immunoglobulin Fab Fragments - chemistry</subject><subject>Immunoglobulin Fab Fragments - therapeutic use</subject><subject>Immunoglobulin Fc Fragments - analysis</subject><subject>Immunoglobulin Fc Fragments - chemistry</subject><subject>Immunoglobulin Fc Fragments - therapeutic use</subject><subject>Immunoglobulin G - analysis</subject><subject>Immunoglobulin G - chemistry</subject><subject>Immunoglobulin G - therapeutic use</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Methionine - analogs & derivatives</subject><subject>Methionine - analysis</subject><subject>Methionine - chemistry</subject><subject>Nanotechnology</subject><subject>Neurobiology</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Oxidative Stress</subject><subject>Proteins</subject><subject>Quantitative Structure-Activity Relationship</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Spectrum 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Oxidation is one of the most common causes of degradation and is typically associated with impairment of the native protein structure. Methionine residues stand out as particularly susceptible to oxidation by reactive oxygen intermediates even under mild conditions. Consequently, methionine oxidation has profound effects on protein activity up to the point of adverse biological responses. Of immediate importance therefore is finding affordable approaches for rapid detection of methionine oxidation before any substantial structural changes can ensue. Herein we report that vibrational bands at 1,044 and 1,113 cm
−1
in the mid-infrared region can serve as characteristic markers of methionine oxidation in oxidatively stressed protein therapeutics, monoclonal antibodies (IgG1 and its antigen-binding fragment). Such Fourier-transform infrared (FTIR) markers underpin rapid detection assays and hold particular promise for correlation of methionine oxidation with protein structure and function.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>21229353</pmid><doi>10.1007/s00249-010-0656-1</doi><tpages>7</tpages></addata></record> |
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subjects | Biochemistry Biodegradation Biological and Medical Physics Biomarkers - analysis Biomarkers - chemistry Biomedical and Life Sciences Biophysics Biophysics Letter Cell Biology Circular Dichroism - methods Fourier transforms Immunoglobulin Fab Fragments - analysis Immunoglobulin Fab Fragments - chemistry Immunoglobulin Fab Fragments - therapeutic use Immunoglobulin Fc Fragments - analysis Immunoglobulin Fc Fragments - chemistry Immunoglobulin Fc Fragments - therapeutic use Immunoglobulin G - analysis Immunoglobulin G - chemistry Immunoglobulin G - therapeutic use Life Sciences Membrane Biology Methionine - analogs & derivatives Methionine - analysis Methionine - chemistry Nanotechnology Neurobiology Oxidation Oxidation-Reduction Oxidative Stress Proteins Quantitative Structure-Activity Relationship Spectrometry, Fluorescence Spectroscopy, Fourier Transform Infrared Spectrum analysis |
title | FTIR markers of methionine oxidation for early detection of oxidized protein therapeutics |
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