Mechanical behavior and microstructure of self-assembling oligopeptide gels

Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Mechanical Engineering, 2010.

Bibliographic Details
Main Author: Hammond, Nathan Allen
Other Authors: Roger D. Kamm.
Format: Thesis
Language:eng
Published: Massachusetts Institute of Technology 2011
Subjects:
Online Access:http://hdl.handle.net/1721.1/62510
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author Hammond, Nathan Allen
author2 Roger D. Kamm.
author_facet Roger D. Kamm.
Hammond, Nathan Allen
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description Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Mechanical Engineering, 2010.
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spelling mit-1721.1/625102019-04-12T10:24:21Z Mechanical behavior and microstructure of self-assembling oligopeptide gels Hammond, Nathan Allen Roger D. Kamm. Massachusetts Institute of Technology. Dept. of Mechanical Engineering. Massachusetts Institute of Technology. Dept. of Mechanical Engineering. Mechanical Engineering. Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Mechanical Engineering, 2010. Cataloged from PDF version of thesis. Includes bibliographical references (p. 97-103). Hydrogels have become widely used in the fields of tissue engineering and drug delivery. One class of hydrogel is formed from synthetic oligopeptides that self-assemble into a solution of beta-sheet filaments. These filaments can aggregate to form a gel suitable for culture of various cell types. Examples of such self-assembling peptides are RAD16-I, RAD16-II, and KLD-12. One limitation of self-assembling peptide hydrogels is their mechanical weakness. Herein are presented computational and experimental studies that elucidate the microstructure and mechanical behavior of these materials. Strategies to enhance their mechanical properties are also examined. Steered molecular dynamics modeling was used to characterize the mechanical interaction between filaments, and a coarse-grained model was developed to extend the system to ordinary time scales. A microindentation assay was developed and used to characterize the mechanical properties of gels. Several strategies for enhancing the gels' mechanical properties were tested. Gel microstructure was observed in thin sections of material with transmission electron microscopy, revealing in detail the loose, disorganized structure of assembled beta-sheet filaments. The results demonstrate that these self-assembling peptide gels are formed from a loosely arranged structure of beta-sheet filaments, not from dense bundles of parallel filaments as was previously proposed. Estimates of gel stiffness based on this loose structure are in approximate agreement with experimental measurements. Among the strategies tested to increase gel stiffness, introducing cross-links and increasing solid concentration proved to be effective approaches. by Nathan Allen Hammond. Ph.D. 2011-04-25T16:11:03Z 2011-04-25T16:11:03Z 2010 2010 Thesis http://hdl.handle.net/1721.1/62510 712602173 eng M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission. http://dspace.mit.edu/handle/1721.1/7582 103 p. application/pdf Massachusetts Institute of Technology
spellingShingle Mechanical Engineering.
Hammond, Nathan Allen
Mechanical behavior and microstructure of self-assembling oligopeptide gels
title Mechanical behavior and microstructure of self-assembling oligopeptide gels
title_full Mechanical behavior and microstructure of self-assembling oligopeptide gels
title_fullStr Mechanical behavior and microstructure of self-assembling oligopeptide gels
title_full_unstemmed Mechanical behavior and microstructure of self-assembling oligopeptide gels
title_short Mechanical behavior and microstructure of self-assembling oligopeptide gels
title_sort mechanical behavior and microstructure of self assembling oligopeptide gels
topic Mechanical Engineering.
url http://hdl.handle.net/1721.1/62510
work_keys_str_mv AT hammondnathanallen mechanicalbehaviorandmicrostructureofselfassemblingoligopeptidegels