- Title Information
- Title
- Simulation and Synthesis of Functional, Self-Assembling Amyloid Complexes for the Development of Antimicrobial Coatings
- Type of Resource
- text
- Name:
Personal
- Name Part
- Altemose, Quentin Donald
- Role
- Role Term:
Text
- creator
- Name:
Personal
- Name Part
- Gray, Marissa
- Role
- Role Term:
Text
- Reader
- Name:
Personal
- Name Part
- Borton, David
- Role
- Role Term:
Text
- Reader
- Name:
Personal
- Name Part
- Shukla, Anita
- Role
- Role Term:
Text
- Advisor
- Name:
Corporate
- Name Part
- Brown University. Biology and Medicine: Biomedical Engineering
- Role
- Role Term:
Text
- sponsor
- Origin Information
- Copyright Date
- 2020
- Physical Description
- Extent
- xii, 73 p.
- digitalOrigin
- born digital
- Note:
thesis
- Thesis (Sc. M.)--Brown University, 2020
- Genre (aat)
- theses
- Abstract
- Infections borne from the implantation of medical devices has continued to be a global health concern. Bacteria are capable of binding to the surfaces of these implantable materials, which allows the formation of colonies that secrete a waxy, protective extracellular material known as biofilm, which limits the ability for healthcare providers to treat the infection after it is established. The presence of the biofilm prevents immune cells from phagocytosing the bacteria, while simultaneously blocking antigen receptors on the surface of bacteria, preventing attachment and function of antibiotic drugs. Current methods of preventing bacterial attachment on medical devices include the coating of said devices in antimicrobial films that either repel or kill bacteria on contact. Many of these films however are short-lived, degrading rapidly in aqueous environments. Additionally, many of these materials are limited in what bacterial targets they are capable of treating. In order to address these problems, we have developed a novel self-assembled material capable of binding and releasing targeted ligand drug molecules. Here, we present a novel peptide sequence capable of forming amyloid fibrils as well as binding to targeted, antimicrobial ligands. Our peptide was able to self-assemble and form amyloid fibrils in vitro as determined by Congo Red and Thioflavin T staining. Our self-assembled fibrils are shown to bind to the antibiotic agent gentamicin, preventing the adhesion of bacteria onto glass surfaces. Furthermore, upon exposure to a specific release molecule (e.g. curcumin), the self-assembled fibrils are shown to release gentamicin into the surrounding environment. This has significant implications for the future development of antimicrobial coatings on medical devices.
- Subject (fast)
(authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/01024734")
- Topic
- Molecular biology
- Subject
- Topic
- Self-assembly
- Subject (fast)
(authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/01057564")
- Topic
- Peptides
- Subject
- Topic
- antibacterial biomaterials
- Subject (fast)
(authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/00832028")
- Topic
- Bioengineering
- Subject (fast)
(authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/00865859")
- Topic
- Coatings
- Subject (fast)
(authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/00998460")
- Topic
- Ligand binding (Biochemistry)
- Subject (fast)
(authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/01057580")
- Topic
- Peptides--Synthesis
- Subject
- Topic
- amyloids
- Subject (fast)
(authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/00825153")
- Topic
- Bacteria--Adhesion
- Subject (fast)
(authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/01057565")
- Topic
- Peptides--Analysis
- Language
- Language Term (ISO639-2B)
- English
- Record Information
- Record Content Source (marcorg)
- RPB
- Record Creation Date
(encoding="iso8601")
- 20200720
- Identifier:
DOI
- 10.26300/9ydh-kc65
- Access Condition:
rights statement
(href="http://rightsstatements.org/vocab/InC/1.0/")
- In Copyright
- Access Condition:
restriction on access
- Collection is open for research.