The impacts of solvation and segment variations on the structures of amyloid-beta

dc.contributor.advisorCoskuner, Orkid
dc.contributor.authorKitahara, Taizo
dc.contributor.committeeMemberKurtz, Donald
dc.contributor.committeeMemberPerry, George
dc.date.accessioned2024-02-12T14:41:18Z
dc.date.available2024-02-12T14:41:18Z
dc.date.issued2011
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.abstractAmyloid-beta (Abeta) is a disordered peptide and is at the center of cerebral amyloid angiopathy and Alzheimer's disease. Currently, the impacts of solvation and segment variation on the structures of Abeta are poorly understood. A large amount of human body consists of water and solvation effects can influence the disordered peptide structure. Furthermore, segment variations including different fragment sizes and mutation have been related to Alzheimer's disease. We performed molecular dynamics simulations coupled with thermodynamic calculations and special sampling techniques to elucidate the impacts of solvation and segment variations on Abeta structures. Various smaller fragment sizes of Abeta have been utilized to mimic the properties of the full-length Abeta peptide. Among these, the widely used smaller fragment peptides are Abeta16 and Abeta28. Our studies show that the Asp1-Lys16 and Asp1-Asp28 regions of the full length Abeta42 peptide cannot be completely mimicked by studying the Abeta16 and Abeta28 peptides in an aqueous solution environment. Our studies indicate that Arg5 plays significant roles in the intra-molecular interactions of the wild type Abeta peptide. The mutation of Arg with Ala impacts the structures of the wild-type peptide. Even though the secondary and tertiary structure properties of the R5A mutant are different from those of wild type Abeta42 peptides in aqueous medium, the conformational Gibbs free energies are similar. The results provide the lacking knowledge of the impacts of solvation and segment variations on the structures of Abeta at atomic level with dynamics and can be useful for the fundamental understanding of the properties of Abeta and for designing more efficient treatments for Alzheimer's disease.
dc.description.departmentChemistry
dc.format.extent104 pages
dc.format.mimetypeapplication/pdf
dc.identifier.urihttps://hdl.handle.net/20.500.12588/4101
dc.languageen
dc.subject
dc.subjectAbeta
dc.subjectAMYLOID-β
dc.subjectAmyloid-beta
dc.subjectArg
dc.subjectfragment
dc.subjectsolvation
dc.subject.classificationPhysical chemistry
dc.subject.classificationMolecular chemistry
dc.subject.classificationMolecular biology
dc.subject.classificationBiophysics
dc.subject.classificationTheoretical physics
dc.titleThe impacts of solvation and segment variations on the structures of amyloid-beta
dc.typeThesis
dc.type.dcmiText
dcterms.accessRightspq_closed
thesis.degree.departmentChemistry
thesis.degree.grantorUniversity of Texas at San Antonio
thesis.degree.levelMasters
thesis.degree.nameMaster of Science

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