Novel combinations of experimental and computational analysis tested on the binding of metalloprotoporphyrins to albumin

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dc.contributor.authorHu, Jie
dc.contributor.authorSoraiz, Eduardo Hernandez
dc.contributor.authorJohnson, Courtney N.
dc.contributor.authorDemeler, Borries
dc.contributor.authorBrancaleon, Lorenzo
dc.date.accessioned2021-08-20T22:39:48Z
dc.date.available2021-08-20T22:39:48Z
dc.date.issued2019
dc.descriptionAccepted author manuscripten_US
dc.description.abstractThe evidence that Human Serum Albumin (HSA) binds metal ions and organometallic compounds has generated interest in its physiological role as a metalloprotein and as a vehicle for synthetic biology applications (e.g., synthetic blood and solar energy conversion). HSA has been shown to bind metallo-porphyrins, however, the structural details of such interactions are available only for the HSA:heme complex. A typical challenge for studying the interaction of proteins with metalloporphyrins is the poor solubility of the ligands that affect the characterization the complexes. The manuscript shows that a combination of dialysis and centrifugation yields aqueous solutions that contain >90% HSA:porphyrin complexes and virtually eliminate aggregated ligands. The removal of aggregates increases the quality of the optical spectroscopy data which, in turn, yield more accurate binding constants (~0.1 and 2.1 × 106 M−1) and reveal FRET between Trp214 and the porphyrins. The Trp-porphyrin distance was estimated to be within the 28–34 Å range and was used to guide the search of binding sites through a novel feedback approach with docking simulations. Results suggest while some protoporphyrins (metal-free, Fe(III)PPIX and Mg(II)PPIX) bind HSA at the heme site, others (Zn(II)PPIX, Mn(III)PPIX and Sn(IV)PPIX) are more likely to bind the Cys34.en_US
dc.description.peer-reviewYesen_US
dc.identifier.citationHu, J., Soraiz, E. H., Johnson, C. N., Demeler, B., & Brancaleon, L. (2019). Novel combinations of experimental and computational analysis tested on the binding of metalloprotoporphyrins to albumin. International Journal of Biological Macromolecules, 134(1), 445-457. https://doi.org/10.1016/j.ijbiomac.2019.05.060en_US
dc.identifier.urihttps://hdl.handle.net/10133/6008
dc.language.isoen_USen_US
dc.publisherElsevieren_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionUniversity of Texas at San Antonioen_US
dc.publisher.institutionUniversity of Texas Health Science Center at San Antonioen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.urlhttps://doi.org/10.1016/j.ijbiomac.2019.05.060en_US
dc.subjectMetalloporphyrins
dc.subjectAggregates
dc.subjectAlbumin
dc.subject.lcshDialysis
dc.subject.lcshCentrifugation
dc.titleNovel combinations of experimental and computational analysis tested on the binding of metalloprotoporphyrins to albuminen_US
dc.typeArticleen_US
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