Home
Resource
Investigation of negatively charged biopolymers for stabilizing enzymes and preventing aggregation
PDF
PDF format is widely accepted and good for printing.
Plug-in required
PDF-1(1.49 MB)
Citation & Export
View Usage Statistics
Staff View

Citation & Export
Hide

Simple citation

Nguyen, Kaitlyn. Investigation of negatively charged biopolymers for stabilizing enzymes and preventing aggregation. Retrieved from https://doi.org/doi:10.7282/t3-6ndz-ah51

Export

Click here for information about Citation Management Tools at Rutgers.

Statistics
Hide

Description

TitleInvestigation of negatively charged biopolymers for stabilizing enzymes and preventing aggregation
NameNguyen, Kaitlyn (author); Fu, Jinglin (chair); Zhu, Hao (member); Salas-De La Cruz, David (member); Rutgers University; Graduate School - Camden
Date Created2022
Other Date2022-05 (degree)
SubjectChemistry, Biopolymers
Extent68 pages : illustrations
DescriptionProteins and peptides are macromolecules involved in most function processes within cells of living organisms. Proteins provide functional and structural support, such as catalyzing biochemical reactions, serving as sources of energy, and maintaining cell shapes. However, sometimes, proteins cannot be folded accurately due to cellular synthesis mistakes or disrupted by other molecules. Misfolded or aggregated proteins become toxic to cells and can cause many neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, and Huntington's disease. Thus, it is important to develop molecules and methods that can reduce aggregated proteins. In this thesis, first, I studied how short peptides selected from microarray screening were able to inhibit enzymes and to trigger the aggregation of enzymes. Peptide-protein aggregations were characterized by bioactivity assays and structural analysis of dynamic light scattering and atomic force microscope. Further studies showed that peptide-protein aggregations could be reduced by adding negatively charged biopolymers of polyphosphates, ssDNA, and low pI peptides, possibly due to the disruption of the electrostatic interaction between peptides and proteins in the aggregation. Moreover, these biopolymers were able to recover the activity of aggregated and inhibited peptide/β-Gal complex. Negatively charged biopolymers could also serve as chaperones to stabilize the enzymes at higher temperatures. They could be used in high-throughput screening assays to reduce peptides/protein aggregation and thereby minimize promiscuous inhibitions, or work as protein chaperones.
NoteM.S.
NoteIncludes bibliographical references
Genretheses
Persistent URLhttps://doi.org/doi:10.7282/t3-6ndz-ah51
LanguageEnglish
CollectionCamden Graduate School Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.
Version 8.5.5
Rutgers University Libraries - Copyright ©2024