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dc.rights.licenseRestricted to current Rensselaer faculty, staff and students. Access inquiries may be directed to the Rensselaer Libraries.
dc.contributorKarande, Pankaj
dc.contributorGarde, Shekhar
dc.contributorCramer, Steven M.
dc.contributorGross, Richard
dc.contributorLee, Sangwoo.
dc.contributor.authorKwak, Junha (John)
dc.date.accessioned2021-11-03T08:49:16Z
dc.date.available2021-11-03T08:49:16Z
dc.date.created2017-07-03T14:32:27Z
dc.date.issued2017-05
dc.identifier.urihttps://hdl.handle.net/20.500.13015/1965
dc.descriptionMay 2017
dc.descriptionSchool of Engineering
dc.description.abstractWe investigated calcium oxalate monohydrate (COM), found in plants and kidney stones, as a model system of crystallization. We studied the effects of four common proteins on COM crystallization: bovine serum albumin (BSA), transferrin, lactoferrin, and lysozyme. Through kinetic studies of COM crystallization, we classified BSA and lysozyme as COM growth inhibitor and promoter respectively. Their inhibition and promotion effects were also evident in the macroscopic crystal habit. Through adsorption and microscopy experiments, we showed that BSA exhibits binding specificity for the apical surfaces of macroscopic COM crystals. Lysozyme, on the other, functions via a non-binding mechanism at the surface to accelerate the growth of the apical surfaces. We also synthesized and studied peptides derived from the protein primary sequences to identify putative domains responsible for these inhibition and promotion effects. Collectively, our study of physiologically relevant biomolecules suggests potential roles of COM modifiers in pathological crystallization and helps to develop guidelines for rational design of biomolecular growth modifiers for applications in crystal engineering.
dc.description.abstractCrystallization processes are ubiquitous in nature, science, and technology. Controlling crystal growth is pivotal in many industries as material properties and functions can be tailored by tuning crystal habits (e.g. size, shape, phase). In biomineralization, organisms exert excellent control over bottom-up synthesis and assembly of inorganic-organic structures (e.g. bones, teeth, exoskeletons). This is made possible by growth modifiers that range from small molecules to macromolecules, such as proteins. Molecular recognition of the mineral phase allows proteins to function as nucleation templates, matrices, and growth inhibitors or promoters. We are interested in taking a biomimetic approach to control crystallization via biomolecular growth modifiers.
dc.language.isoENG
dc.publisherRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofRensselaer Theses and Dissertations Online Collection
dc.subjectChemical engineering
dc.titleA study of biomolecules as growth modifiers of calcium oxalate crystals
dc.typeElectronic thesis
dc.typeThesis
dc.digitool.pid178246
dc.digitool.pid178247
dc.digitool.pid178248
dc.rights.holderThis electronic version is a licensed copy owned by Rensselaer Polytechnic Institute, Troy, NY. Copyright of original work retained by author.
dc.description.degreePhD
dc.relation.departmentDept. of Chemical and Biological Engineering


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