Characterization of photophysical properties and structural effects of various protoporphyrins docked to human serum albumin preliminary study for future solar energy conversion applications

dc.contributor.advisorBrancaleon, Lorenzo
dc.contributor.authorHu, Jie
dc.contributor.committeeMemberBrancaleon, Lorenzo
dc.contributor.committeeMemberChen, Chonglin
dc.contributor.committeeMemberNegrete, George R.
dc.contributor.committeeMemberNash, Kelly
dc.contributor.committeeMemberPonce, Arturo
dc.date.accessioned2024-02-09T22:22:56Z
dc.date.available2024-02-09T22:22:56Z
dc.date.issued2016
dc.descriptionThis item is available only to currently enrolled UTSA students, faculty or staff. To download, navigate to Log In in the top right-hand corner of this screen, then select Log in with my UTSA ID.
dc.description.abstractPhotosensitized processes as a way to prompt changes in natural as well as engineered biomolecules have received increasing interest for the manipulation of biomaterials. In this study, we present the photo-physical properties of the interaction between HSA and various photosensitizers, including free base PPIX and metal-chelated PPIX compounds (Zn(II)PPIX, Hemin, Mg(II)PPIX, Mn(III)PPIX and Sn(IV)PPIX). A primary obstacle in the study has been the poor solubility of the porphyrins in aqueous solution. Fortunately, we’ve been able to develop an effective improved sample preparation method to eliminate or reduce this aggregation effect, which reveals the occurrence of Förster Resonance Energy Transfer (FRET) when the porphyrins (acceptor molecule) bound to the HSA (donor molecule), based on the donor molecule has an emission spectrum that substantially overlaps with the absorption spectrum of the acceptor and the fluorescence lifetime decay spectra as well. FRET analysis provides a series of donor-acceptor distance in good agreement with the results of similar complexes resolved by X-ray diffraction. These results are used to guide the computational docking simulations, indicating the most favorable docking site for each protoporphyrin respectively. In addition, to study the photo-event induced by photosensitizers on the protein, the irradiation experiments are performed with a 405nm diode laser. Besides the absorption, fluorescence and lifetime spectroscopic data, Circular Dichroism (CD) spectra are also recorded and analyzed to establish the extent of the changes of the secondary structure of the protein upon irradiation. Overall, the study provides a significant step forward in the field of photosensitized protein engineering.
dc.description.departmentPhysics and Astronomy
dc.format.extent175 pages
dc.format.mimetypeapplication/pdf
dc.identifier.isbn9781369441079
dc.identifier.urihttps://hdl.handle.net/20.500.12588/3845
dc.languageen
dc.subjectdocking
dc.subjectFRET
dc.subjectHuman Serum Albumin
dc.subjectirradiation
dc.subjectphotoinduced effect
dc.subjectprotoporphyrins
dc.subject.classificationPhysics
dc.subject.classificationBiophysics
dc.titleCharacterization of photophysical properties and structural effects of various protoporphyrins docked to human serum albumin preliminary study for future solar energy conversion applications
dc.typeThesis
dc.type.dcmiText
dcterms.accessRightspq_closed
thesis.degree.departmentPhysics and Astronomy
thesis.degree.grantorUniversity of Texas at San Antonio
thesis.degree.levelDoctoral
thesis.degree.nameDoctor of Philosophy

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