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Structural changes of human serum albumin immobilized on chromatographic supports: a high-performance liquid chromatography and Fourier-transform infrared spectroscopy study
Chiral stationary phases obtained by immobilization of HSA on [C8] and [C18] reversed-phases and on poly(1-vinylimidazole)-coated silica were tested to resolve dl-tryptophan, N-benzoyl- dl-phenylalanine, RS-oxazepam and RS-warfarin racemic mixtures. Parameters of enantioselectivity measured in HPLC...
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| Published in: | Journal of chromatography. B, Biomedical sciences and applications Biomedical sciences and applications, 2001-03, Vol.753 (1), p.101-113 |
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| Main Authors: | , , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c423t-7d6b7307199a56e675b4153d184b0fc853b866067a979f38d1760394347bf6643 |
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| cites | cdi_FETCH-LOGICAL-c423t-7d6b7307199a56e675b4153d184b0fc853b866067a979f38d1760394347bf6643 |
| container_end_page | 113 |
| container_issue | 1 |
| container_start_page | 101 |
| container_title | Journal of chromatography. B, Biomedical sciences and applications |
| container_volume | 753 |
| creator | Millot, M.C Servagent-Noinville, S Taleb, N.L Baron, M.H Revault, M Sébille, B |
| description | Chiral stationary phases obtained by immobilization of HSA on [C8] and [C18] reversed-phases and on poly(1-vinylimidazole)-coated silica were tested to resolve
dl-tryptophan,
N-benzoyl-
dl-phenylalanine,
RS-oxazepam and
RS-warfarin racemic mixtures. Parameters of enantioselectivity measured in HPLC are correlated to structural and solvation states for adsorbed HSA, evaluated by FTIR spectroscopy. HSA immobilized on [PVI]-anion-exchangers is highly selective. HSA molecules are not self-associated, only unfolded for a small hydrophobic helix. The HSA-coated reversed-phases have a lower selectivity. Unfolding is larger but the indole-benzodiazepine chiral site is preserved and remains accessible. |
| doi_str_mv | 10.1016/S0378-4347(00)00424-2 |
| format | article |
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dl-tryptophan,
N-benzoyl-
dl-phenylalanine,
RS-oxazepam and
RS-warfarin racemic mixtures. Parameters of enantioselectivity measured in HPLC are correlated to structural and solvation states for adsorbed HSA, evaluated by FTIR spectroscopy. HSA immobilized on [PVI]-anion-exchangers is highly selective. HSA molecules are not self-associated, only unfolded for a small hydrophobic helix. The HSA-coated reversed-phases have a lower selectivity. Unfolding is larger but the indole-benzodiazepine chiral site is preserved and remains accessible.</description><identifier>ISSN: 0378-4347</identifier><identifier>ISSN: 1387-2273</identifier><identifier>DOI: 10.1016/S0378-4347(00)00424-2</identifier><identifier>PMID: 11302435</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Albumins - chemistry ; Analysis ; Biological and medical sciences ; Chemical Sciences ; Chromatography, High Pressure Liquid - methods ; General pharmacology ; Human serum albumin ; Humans ; Medical sciences ; Pharmacology. Drug treatments ; Protein Conformation ; Spectroscopy, Fourier Transform Infrared - methods</subject><ispartof>Journal of chromatography. B, Biomedical sciences and applications, 2001-03, Vol.753 (1), p.101-113</ispartof><rights>2001 Elsevier Science B.V.</rights><rights>2001 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c423t-7d6b7307199a56e675b4153d184b0fc853b866067a979f38d1760394347bf6643</citedby><cites>FETCH-LOGICAL-c423t-7d6b7307199a56e675b4153d184b0fc853b866067a979f38d1760394347bf6643</cites><orcidid>0000-0002-8320-9488</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>309,310,314,780,784,789,790,885,23930,23931,25140,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=937129$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11302435$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-03085276$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Millot, M.C</creatorcontrib><creatorcontrib>Servagent-Noinville, S</creatorcontrib><creatorcontrib>Taleb, N.L</creatorcontrib><creatorcontrib>Baron, M.H</creatorcontrib><creatorcontrib>Revault, M</creatorcontrib><creatorcontrib>Sébille, B</creatorcontrib><title>Structural changes of human serum albumin immobilized on chromatographic supports: a high-performance liquid chromatography and Fourier-transform infrared spectroscopy study</title><title>Journal of chromatography. B, Biomedical sciences and applications</title><addtitle>J Chromatogr B Biomed Sci Appl</addtitle><description>Chiral stationary phases obtained by immobilization of HSA on [C8] and [C18] reversed-phases and on poly(1-vinylimidazole)-coated silica were tested to resolve
dl-tryptophan,
N-benzoyl-
dl-phenylalanine,
RS-oxazepam and
RS-warfarin racemic mixtures. Parameters of enantioselectivity measured in HPLC are correlated to structural and solvation states for adsorbed HSA, evaluated by FTIR spectroscopy. HSA immobilized on [PVI]-anion-exchangers is highly selective. HSA molecules are not self-associated, only unfolded for a small hydrophobic helix. The HSA-coated reversed-phases have a lower selectivity. Unfolding is larger but the indole-benzodiazepine chiral site is preserved and remains accessible.</description><subject>Albumins - chemistry</subject><subject>Analysis</subject><subject>Biological and medical sciences</subject><subject>Chemical Sciences</subject><subject>Chromatography, High Pressure Liquid - methods</subject><subject>General pharmacology</subject><subject>Human serum albumin</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Pharmacology. 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Drug treatments</topic><topic>Protein Conformation</topic><topic>Spectroscopy, Fourier Transform Infrared - methods</topic><toplevel>online_resources</toplevel><creatorcontrib>Millot, M.C</creatorcontrib><creatorcontrib>Servagent-Noinville, S</creatorcontrib><creatorcontrib>Taleb, N.L</creatorcontrib><creatorcontrib>Baron, M.H</creatorcontrib><creatorcontrib>Revault, M</creatorcontrib><creatorcontrib>Sébille, B</creatorcontrib><collection>Pascal-Francis</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><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Journal of chromatography. 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dl-tryptophan,
N-benzoyl-
dl-phenylalanine,
RS-oxazepam and
RS-warfarin racemic mixtures. Parameters of enantioselectivity measured in HPLC are correlated to structural and solvation states for adsorbed HSA, evaluated by FTIR spectroscopy. HSA immobilized on [PVI]-anion-exchangers is highly selective. HSA molecules are not self-associated, only unfolded for a small hydrophobic helix. The HSA-coated reversed-phases have a lower selectivity. Unfolding is larger but the indole-benzodiazepine chiral site is preserved and remains accessible.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>11302435</pmid><doi>10.1016/S0378-4347(00)00424-2</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0002-8320-9488</orcidid></addata></record> |
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| identifier | ISSN: 0378-4347 |
| ispartof | Journal of chromatography. B, Biomedical sciences and applications, 2001-03, Vol.753 (1), p.101-113 |
| issn | 0378-4347 1387-2273 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77049800 |
| source | ScienceDirect Freedom Collection |
| subjects | Albumins - chemistry Analysis Biological and medical sciences Chemical Sciences Chromatography, High Pressure Liquid - methods General pharmacology Human serum albumin Humans Medical sciences Pharmacology. Drug treatments Protein Conformation Spectroscopy, Fourier Transform Infrared - methods |
| title | Structural changes of human serum albumin immobilized on chromatographic supports: a high-performance liquid chromatography and Fourier-transform infrared spectroscopy study |
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