Designer metal-triggered collagen peptides
Abstract
Self-assembling systems provide unique bottom up approaches for creating nano- to macro-sized materials. These materials can be given discrete biological functions, serve as drug delivery systems, and can be used in regenerative medicines. While a variety of unique self-assembling peptide systems, including beta sheet peptides and peptide amphiphiles, have successfully been developed, collagen based self-assembling systems offer the closest mimic to creating a synthetic extracellular matrix. To achieve such a system, one must first control the spatial and physical properties of the self-assembling system. We have successfully designed and synthesized two unique metal-triggered, self-assembling peptide systems (NHbipy and H-(byp) n) that can assemble in both linear and radial directions. Radial assembly was utilized in the H(byp)n system leading to the formation of fibers, disks, and hollow spheres. NHbipy incorporated both radial and linear assembly strategies, resulting in a dense fibrous scaffold capable of three-dimensional cell culture with a variety of different cell lines. This assembly process also allowed for the incorporation of functionalized collagen peptides that provided enhanced biological properties and programmable morphological controls over the 3-dimensional environment of the collagen scaffold. These features demonstrate the adaptive versatility of the NHbipy scaffold and its potential applications in regenerative medicine.
Degree
Ph.D.
Advisors
Chmielewski, Purdue University.
Subject Area
Biochemistry|Organic chemistry
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