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Chromatographic separation simulation of metal‐chelating peptides from surface plasmon resonance binding parameters
Some metal‐chelating peptides have antioxidant properties, with potential nutrition, health, and cosmetics applications. This study aimed to simulate their separation on immobilized metal ion affinity chromatography from their affinity constant for immobilized metal ion determined in surface plasmon...
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Published in: | Journal of separation science 2020-06, Vol.43 (11), p.2031-2041 |
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creator | Muhr, Laurence Pontvianne, Steve Selmeczi, Katalin Paris, Cédric Boschi‐Muller, Sandrine Canabady‐Rochelle, Laetitia |
description | Some metal‐chelating peptides have antioxidant properties, with potential nutrition, health, and cosmetics applications. This study aimed to simulate their separation on immobilized metal ion affinity chromatography from their affinity constant for immobilized metal ion determined in surface plasmon resonance, both technics are based on peptide‐metal ion interactions. In our approach, first, the affinity constant of synthetic peptides was determined by surface plasmon resonance and used as input data to numerically simulate the chromatographic separation with a transport‐dispersive model based on Langmuir adsorption isotherm. Then, chromatographic separation was applied on the same peptides to determine their retention time and compare this experimental tR with the simulated tR obtained from simulation from surface plasmon resonance data. For the investigated peptides, the relative values of tR were comparable. Hence, our study demonstrated the pertinence of such numerical simulation correlating immobilized metal ion affinity chromatography and surface plasmon resonance. |
doi_str_mv | 10.1002/jssc.201900882 |
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This study aimed to simulate their separation on immobilized metal ion affinity chromatography from their affinity constant for immobilized metal ion determined in surface plasmon resonance, both technics are based on peptide‐metal ion interactions. In our approach, first, the affinity constant of synthetic peptides was determined by surface plasmon resonance and used as input data to numerically simulate the chromatographic separation with a transport‐dispersive model based on Langmuir adsorption isotherm. Then, chromatographic separation was applied on the same peptides to determine their retention time and compare this experimental tR with the simulated tR obtained from simulation from surface plasmon resonance data. For the investigated peptides, the relative values of tR were comparable. Hence, our study demonstrated the pertinence of such numerical simulation correlating immobilized metal ion affinity chromatography and surface plasmon resonance.</description><identifier>ISSN: 1615-9306</identifier><identifier>EISSN: 1615-9314</identifier><identifier>DOI: 10.1002/jssc.201900882</identifier><identifier>PMID: 32125758</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Adsorption ; Affinity ; Antioxidants ; Chelating Agents - chemistry ; Chelating Agents - isolation & purification ; Chelation ; Chemical Sciences ; Chromatography ; Chromatography, Affinity ; Computer simulation ; Cosmetics ; Engineering Sciences ; immobilized metal ion affinity chromatography ; Ions ; Mathematical models ; Metal ions ; modeling ; Nutrition ; Peptides ; Peptides - chemistry ; Peptides - isolation & purification ; Separation ; Simulation ; Surface Plasmon Resonance ; Transition Elements - chemistry ; Transition Elements - isolation & purification</subject><ispartof>Journal of separation science, 2020-06, Vol.43 (11), p.2031-2041</ispartof><rights>2020 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2020 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4790-cfd614e93b22c529fa9a93d27fdf7ad1f51900a07391d4ae46a2479040cd1d3b3</citedby><cites>FETCH-LOGICAL-c4790-cfd614e93b22c529fa9a93d27fdf7ad1f51900a07391d4ae46a2479040cd1d3b3</cites><orcidid>0000-0003-2772-1556 ; 0000-0001-8673-3130 ; 0000-0003-3291-3309 ; 0000-0003-1177-0329 ; 0000-0001-8962-4749</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32125758$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02938784$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Muhr, Laurence</creatorcontrib><creatorcontrib>Pontvianne, Steve</creatorcontrib><creatorcontrib>Selmeczi, Katalin</creatorcontrib><creatorcontrib>Paris, Cédric</creatorcontrib><creatorcontrib>Boschi‐Muller, Sandrine</creatorcontrib><creatorcontrib>Canabady‐Rochelle, Laetitia</creatorcontrib><title>Chromatographic separation simulation of metal‐chelating peptides from surface plasmon resonance binding parameters</title><title>Journal of separation science</title><addtitle>J Sep Sci</addtitle><description>Some metal‐chelating peptides have antioxidant properties, with potential nutrition, health, and cosmetics applications. This study aimed to simulate their separation on immobilized metal ion affinity chromatography from their affinity constant for immobilized metal ion determined in surface plasmon resonance, both technics are based on peptide‐metal ion interactions. In our approach, first, the affinity constant of synthetic peptides was determined by surface plasmon resonance and used as input data to numerically simulate the chromatographic separation with a transport‐dispersive model based on Langmuir adsorption isotherm. Then, chromatographic separation was applied on the same peptides to determine their retention time and compare this experimental tR with the simulated tR obtained from simulation from surface plasmon resonance data. For the investigated peptides, the relative values of tR were comparable. 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subjects | Adsorption Affinity Antioxidants Chelating Agents - chemistry Chelating Agents - isolation & purification Chelation Chemical Sciences Chromatography Chromatography, Affinity Computer simulation Cosmetics Engineering Sciences immobilized metal ion affinity chromatography Ions Mathematical models Metal ions modeling Nutrition Peptides Peptides - chemistry Peptides - isolation & purification Separation Simulation Surface Plasmon Resonance Transition Elements - chemistry Transition Elements - isolation & purification |
title | Chromatographic separation simulation of metal‐chelating peptides from surface plasmon resonance binding parameters |
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