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Molecular Level Investigations of the Inter- and Intramolecular Interactions of pH-Responsive Artificial Triblock Proteins

Stevens, Molly M. and Allen, Stephanie and Davies, Martyn C. and Roberts, Clive J. and Sakata, Jill K. and Tendler, Saul J. B. and Tirrell, David A. and Williams, Philip M. (2005) Molecular Level Investigations of the Inter- and Intramolecular Interactions of pH-Responsive Artificial Triblock Proteins. Biomacromolecules, 6 (3). pp. 1266-1271. ISSN 1525-7797. http://resolver.caltech.edu/CaltechAUTHORS:20150114-121449462

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Abstract

Intelligent materials that can undergo physical gelation in response to environmental stimuli have potential impacts in the bioengineering and biomedical fields where the entrapment of cellular or molecular species is desired. Here, we utilize atomic force microscopy (AFM) to perform molecular level investigations of designer artificial proteins that undergo physical gelation. These are engineered as triblock copolymers with independent interchain binding and solvent retention functions, namely, two terminal leucine zipper-like peptide sequences and a central alanylglycine rich sequence, respectively. AFM force measurements between probes and surfaces functionalized with molecules of this triblock protein revealed adhesive interactions that increased in average force and frequency as the pH was lowered from pH 11.2 to 7.4 to 4.5, reflecting an increase in the numbers of interacting molecular strands. In bulk solution, lowering the pH results in a viscous liquid to gel transition. The modular design of the triblock protein was also exploited for single molecule force spectroscopy investigations, which revealed altered intramolecular interactions in response to changes in pH. An increased understanding of the inter- and intramolecular forces involved in biomolecule driven gelation processes is not only of great fundamental interest in the study of the biomolecular systems involved but may also prove key in enabling the rational design of new generations of intelligent hydrogel systems.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/bm049369xDOIArticle
http://pubs.acs.org/doi/abs/10.1021/bm049369xPublisherArticle
ORCID:
AuthorORCID
Tirrell, David A.0000-0003-3175-4596
Additional Information:Copyright © 2005 American Chemical Society. Published In Issue May 09, 2005. Publication Date (Web): March 17, 2005. Received October 6, 2004. Revised Manuscript Received January 28, 2005. Acknowledgment. The authors thank Prof. H. E. Gaub (Ludwig-Maximilians-Universita¨t, Munich) for access to custom-built AFM instrumentation during the early stages of this study. Work at Nottingham was supported by the BBSRC, and S.A. thanks Pfizer Global Research and Development (Sandwich, Kent, UK) for the funding of her lectureship. Work at Caltech was supported by the NSF Center for the Science and Engineering of Materials.
Funders:
Funding AgencyGrant Number
BBSRCUNSPECIFIED
Pfizer Global Research and Development (Sandwich, Kent, UK)UNSPECIFIED
NSF Center for the Science and Engineering of Materials UNSPECIFIED
Record Number:CaltechAUTHORS:20150114-121449462
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20150114-121449462
Official Citation: Molecular Level Investigations of the Inter- and Intramolecular Interactions of pH-Responsive Artificial Triblock Proteins Molly M. Stevens,†,‡, Stephanie Allen,*,†, Martyn C. Davies,†, Clive J. Roberts,†, Jill K. Sakata,§,‖, Saul J. B. Tendler,†, David A. Tirrell,+ and, and Philip M. Williams† Biomacromolecules 2005 6 (3), 1266-1271
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:53711
Collection:CaltechAUTHORS
Deposited By: Katherine Johnson
Deposited On:15 Jan 2015 18:51
Last Modified:15 Jan 2015 18:51

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