Predicting the behaviour of proteins in hydrophobic interaction chromatography 1: using the hydrophobic imbalance (hi) to describe their surface amino acid distribution

JOURNAL OF CHROMATOGRAPHY A;
J. Chromatogr. A

dc.creatorAsenjo-De Leuze, Juan
dc.creatorSalgado-Herrera, José
dc.creatorRapaport-Zimermann, Ivan
dc.date2017-04-27T18:52:21Z
dc.date2022-07-07T02:23:40Z
dc.date2017-04-27T18:52:21Z
dc.date2022-07-07T02:23:40Z
dc.date2006
dc.date.accessioned2023-08-22T00:14:17Z
dc.date.available2023-08-22T00:14:17Z
dc.identifier0
dc.identifierD01I1031
dc.identifierD01I1031
dc.identifierWOS:000235505100014
dc.identifier0021-9673
dc.identifierhttps://hdl.handle.net/10533/197648
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8299589
dc.descriptionThis paper focuses on the prediction of the dimensionless retention time of proteins (DRT) in hydrophobic interaction chromatography (HIC) by means of mathematical models based on characteristics of the surface hydrophobicity distribution. We introduce a new parameter, called hydrophobic imbalance (HI), obtained from the three-dimensional structure of proteins. This parameter quantifies the displacement of the superficial geometric centre of the protein when the effect of the hydrophobicity of each amino acid is considered. This parameter is simpler and less expensive than those reported previously. We use HI as a way to incorporate information about the surface hydrophobicity distribution in order to improve the prediction of DRT. We tested the performance of our DRT predictive models in a set of 15 proteins. This set includes four proteins whose DRTs are known as very difficult to predict. By means of the variable HI, it was possible to improve the predictive characteristics obtained by models based on the average surface hydrophobicity (ASH) by 9.1 %. Also, we studied linear multivariable models based on characteristics determined from the HI. By using this multivariable model, a correlation coefficient of 0.899 was obtained. With this model, we managed to improve the predictive characteristics shown by previous models based on ASH by 31.8%. (c) 2005 Elsevier B.V. All rights reserved.
dc.description0
dc.description20
dc.descriptionFONDEF
dc.descriptionjsalgado@ing.uchile-cl
dc.description0
dc.description1
dc.descriptionFONDEF
dc.description1107
dc.languageENG
dc.publisherELSEVIER SCIENCE BV
dc.relationinstname: Conicyt
dc.relationreponame: Repositorio Digital RI2.0
dc.relationinstname: Conicyt
dc.relationreponame: Repositorio Digital RI2.0
dc.relationinfo:eu-repo/grantAgreement/Fondef/D01I1031
dc.relationinfo:eu-repo/semantics/dataset/hdl.handle.net/10533/93477
dc.relationhttps://doi.org/10.1016/j.chroma.2005.12.032
dc.rightsinfo:eu-repo/semantics/openAccess
dc.titlePredicting the behaviour of proteins in hydrophobic interaction chromatography 1: using the hydrophobic imbalance (hi) to describe their surface amino acid distribution
dc.titleJOURNAL OF CHROMATOGRAPHY A
dc.titleJ. Chromatogr. A
dc.typeArticulo
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:eu-repo/semantics/publishedVersion
dc.coverageAMSTERDAM


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