Alexandria Digital Research Library

Tailoring peptide amphiphiles and their assemblies for biomedical applications

Author:
Lin, Brian
Degree Grantor:
University of California, Santa Barbara.Chemistry
Degree Supervisor:
TirrellHawker MatthewCraig VJ
Place of Publication:
[Santa Barbara, Calif.]
Publisher:
University of California, Santa Barbara
Creation Date:
2012
Issued Date:
2012
Topics:
Biomedical engineering, Chemistry, and Materials Science
Keywords:
protein
tissue scaffold
therapeutic
peptide amphiphile
nanofiber
self assembly
Description:

Peptide amphiphiles (PAs) are molecules composed of a peptide conjugated to a hydrophobic moiety, commonly a fatty acid. They closely resemble the structure of naturally occurring lipopeptides, produced by microbes as signaling and antimicrobial agents. The amphiphilic nature of PAs in concert with the large number of discovered functional peptides inspired scientists to exploit this molecular architecture for producing synthetic self-assembled bioactive materials. PA assemblies are sought after for a wide breadth of applications including disease therapy, regenerative medicine, and catalysis. However, with PAs, the peptide chemistry is a double-edged sword. The peptide component contributes significantly to both the activity and self-assembly. The physiochemical properties of different PAs lead to unique aggregation stability and morphological characteristics which are unpredictable, a priori. Therefore it is challenging to design bioactive PAs and control their self-assembly, simultaneously. This limitation slows the development of PAs for medical use.

In this dissertation, methods to control the self-assembly of PAs and the effects of acylating a functional peptide will be discussed. In one part, efforts to direct the self-assembly of PAs into small spherical aggregates, a morphology infrequently observed, will be described. In another section, a strategy to control the stability of PA assemblies will be discussed. In the last section, a pH-responsive membrane perturbing peptide was modified with fatty acid tails and the properties of the resulting PAs will be presented. This dissertation provides some fundamental insight for the use and design of PA self-assemblies.

Format:
Text
Collection(s):
UCSB electronic theses and dissertations
ARK:
ark:/13030/m51v5fmn
Merritt ARK:
ark:/13030/m51v5fmn
Rights:
Inc.icon only.dark In Copyright
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