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dc.contributor.authorBarata, Teresa S
dc.contributor.authorZhang, Cheng
dc.contributor.authorA. Darby, Paul
dc.contributor.authorBrocchini, Steve
dc.contributor.authorZloh, Mire
dc.date.accessioned2016-11-18T15:41:20Z
dc.date.available2016-11-18T15:41:20Z
dc.date.issued2016-06-01
dc.identifier.citationBarata , T S , Zhang , C , A. Darby , P , Brocchini , S & Zloh , M 2016 , ' Identification of excipient-protein interaction hotspots using computational approaches ' , International Journal of Molecular Sciences , vol. 17 , no. 6 , 853 , pp. 853 . https://doi.org/10.3390/ijms17060853
dc.identifier.issn1422-0067
dc.identifier.otherPURE: 10177330
dc.identifier.otherPURE UUID: cbc3a984-7df1-4f8f-bd31-dbcfbda0d196
dc.identifier.otherScopus: 84971518975
dc.identifier.urihttp://hdl.handle.net/2299/17331
dc.description.abstractProtein formulation development relies on the selection of excipients that inhibit protein-protein interactions preventing aggregation. Empirical strategies involve screening many excipient and buffer combinations using force degradation studies. Such methods do not readily provide information on intermolecular interactions responsible for the protective effects of excipients. This study describes a molecular docking approach to screen and rank interactions allowing for the identification of protein-excipients hotspots to aid in the selection of excipients to be experimentally screened. Previously published work with Drosophila Su(dx) was used to develop and validate the computational methodology which was then used to determine the formulation hotspots for Fab A33. Commonly used excipients were examined and compared to the regions in Fab A33 prone to protein-protein interactions that could lead to aggregation. This approach could provide information on a molecular level about the protective interactions of excipients in protein formulations to aid the more rational development of future formulations.en
dc.format.extent20
dc.language.isoeng
dc.relation.ispartofInternational Journal of Molecular Sciences
dc.rightsOpen
dc.subjectmolecular docking; protein–excipient interactions; protein stability; molecular dynamics; Fab formulation
dc.titleIdentification of excipient-protein interaction hotspots using computational approachesen
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionDepartment of Pharmacy, Pharmacology and Postgraduate Medicine
dc.contributor.institutionCentre for Hazard Detection and Protection Research
dc.contributor.institutionMedicinal and Analytical Chemistry
dc.contributor.institutionPsychopharmacology, Drug Misuse and Novel Psychoactive Substances Unit
dc.contributor.institutionCentre for Health Services and Clinical Research
dc.description.statusPeer reviewed
dc.identifier.urlhttp://www.mdpi.com/1422-0067/17/6/853
dc.relation.schoolSchool of Life and Medical Sciences
dc.description.versiontypeFinal Published version
dcterms.dateAccepted2016-06-01
rioxxterms.versionVoR
rioxxterms.versionofrecordhttps://doi.org/10.3390/ijms17060853
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue
herts.rights.accesstypeOpen


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