Home
Resource
Bridging the scales in biomaterials: role of biophysics from atom-scale to nano-scale
PDF
PDF format is widely accepted and good for printing.
Plug-in required
Access to this PDF has been restricted at the author's request. It will be publicly available after April 27, 2024.
Citation & Export
View Usage Statistics
Staff View

Citation & Export
Hide

Simple citation

Banerjee, Akash. Bridging the scales in biomaterials: role of biophysics from atom-scale to nano-scale. Retrieved from https://doi.org/doi:10.7282/t3-7037-zj18

Export

Click here for information about Citation Management Tools at Rutgers.

Statistics
Hide

Description

TitleBridging the scales in biomaterials: role of biophysics from atom-scale to nano-scale
NameBanerjee, Akash (author); Dutt, Meenakshi (chair); Olson, Wilma Dr. (member); Jha, Shantenu Dr. (member); Chen, Chun-long Dr. (member); Rutgers University; School of Graduate Studies
Date Created2023
Other Date2023-05 (degree)
SubjectComputer science, Biophysics, Computational chemistry, Coarse-grained molecular dynamics, Lipids, Peptides, Peptoids, Workflows
Extent171 pages
DescriptionBiomolecules such as peptides and lipids can self-assemble to form large, ordered structures. These ordered structures form biomaterials that have applications in areas such as biomedicine and electronics. The functionality of these biomaterials can be tuned by modifying the sequence of the biomolecules. To enable the design of such tunable materials with good precision, we need to characterize the biophysics underlying the self- assembly process. At small spatiotemporal scales, the local structure of a biomolecule (for example, the secondary structure of a peptide) governs the intermolecular interactions. At larger spatiotemporal scales, the overall features of the ordered structure (for example, shape, stability, and porosity) govern the functionality of the biomaterial. In this work, a set of computational tools are built to address the self-assembly of biomolecules at multiple scales. First, spherical nanostructures, also known as vesicles, are studied at large spatiotemporal scales. These vesicles encompass polyamidoamine dendron-grafted amphiphiles (PDAs) and dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) lipids. The overall stability of the vesicles is determined as a function of concentration and generation (degree of branching) of PDAs. Next, the local interactions between lipid-like peptides (V6K2, V:Valine and K:Lysine) are studied at small spatiotemporal scales. A model is developed to specifically capture the local structure and chemical details of these peptides. In this way, the organization of a single peptide in a small-sized aggregate is resolved accurately. Furthermore, the model resolves the assembly of these peptides into intermediate-sized aggregates that are in qualitative agreement with experiments. This demonstrates that the technique can resolve the structure (small-scale) and assembly (intermediate-scale) of peptides. Finally, a computational workflow is developed to automate the implementation of these computational tools. This will enable the extension of these tools to different chemical systems, sizes and environmental conditions.
NotePh.D.
NoteIncludes bibliographical references
Genretheses
Persistent URLhttps://doi.org/doi:10.7282/t3-7037-zj18
LanguageEnglish
CollectionSchool of Graduate Studies 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