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dc.contributor.authorTayeb, Hossam H
dc.contributor.authorStienecker, Marina
dc.contributor.authorMiddelberg, Anton PJ
dc.contributor.authorSainsbury, Frank
dc.date.accessioned2020-04-30T00:21:37Z
dc.date.available2020-04-30T00:21:37Z
dc.date.issued2019
dc.identifier.issn0743-7463
dc.identifier.doi10.1021/acs.langmuir.9b01684
dc.identifier.urihttp://hdl.handle.net/10072/393290
dc.description.abstractBiosurfactants are surface active molecules that can be produced by renewable, industrially scalable biologic processes. DAMP4, a designer biosurfactant, enables the modification of interfaces via genetic or chemical fusion to functional moieties. However, bioconjugation of addressable amines introduces heterogeneity that limits the precision of functionalization as well as the resolution of interfacial characterization. Here, we designed DAMP4 variants with cysteine point mutations to allow for site-specific bioconjugation. The DAMP4 variants were shown to retain the structural stability and interfacial activity characteristic of the parent molecule, while permitting efficient and specific conjugation of polyethylene glycol (PEG). PEGylation results in a considerable reduction on the interfacial activity of both single and double mutants. Comparison of conjugates with one or two conjugation sites shows that both the number of conjugates as well as the mass of conjugated material impact the interfacial activity of DAMP4. As a result, the ability of DAMP4 variants with multiple PEG conjugates to impart colloidal stability on peptide-stabilized emulsions is reduced. We suggest that this is due to steric constraints on the structures of amphiphilic helices at the interface. Specific and efficient bioconjugation permits the exploration and investigation of the interfacial properties of designer protein biosurfactants with molecular precision. Our findings should therefore inform the design and modification of biosurfactants for their increasing use in industrial processes and nutritional and pharmaceutical formulations.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherAmerican Chemical Society
dc.relation.ispartofpagefrom13588
dc.relation.ispartofpageto13594
dc.relation.ispartofissue42
dc.relation.ispartofjournalLangmuir
dc.relation.ispartofvolume35
dc.subject.fieldofresearchProteomics and intermolecular interactions (excl. medical proteomics)
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchcode310109
dc.subject.fieldofresearchcode31
dc.subject.keywordsScience & Technology
dc.subject.keywordsPhysical Sciences
dc.subject.keywordsTechnology
dc.subject.keywordsChemistry, Multidisciplinary
dc.subject.keywordsChemistry, Physical
dc.titleImpact of Site-Specific Bioconjugation on the Interfacial Activity of a Protein Biosurfactant
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationTayeb, HH; Stienecker, M; Middelberg, APJ; Sainsbury, F, Impact of Site-Specific Bioconjugation on the Interfacial Activity of a Protein Biosurfactant, Langmuir, 2019, 35 (42), pp. 13588-13594
dc.date.updated2020-04-21T00:10:00Z
dc.description.versionAccepted Manuscript (AM)
gro.rights.copyrightThis document is the Accepted Manuscript version of a Published Work that appeared in final form in Langmuir, copyright 2019 American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.langmuir.9b01684
gro.hasfulltextFull Text
gro.griffith.authorSainsbury, Frank


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