The preparation of hydrogels via peptide self-assembly allows one to define ultimate biomaterial properties by design of individual constituent molecules. Chemical functionality, material morphology, viscoelasticity and processibility can be designed at the molecular level of a self-assembling system. Herein, peptides are designed to intramolecularly fold in response to external stimuli into beta-hairpin conformations that are capable of self-assembling. Folded hairpins assemble into dilute but rigid hydrogels exhibiting porosity on the nano- to -microscale. Triggered folding allows temporal and spatial control of material formation. Gelation will be triggered by various physiologically relevant stimuli;e.g. pH, salt, calcium ions, temperature and light. The chemically benign folding/self-assembly strategy, and the inherent peptidic nature of the resultant hydrogels, provide a potential tissue engineering substrate for fibroblasts and osteoblasts. Peptide design principles leading to rigid, porous hydrogels capable of supporting cell adhesion and proliferation will be determined by directly observing how peptide structure affects the self-assembly process, material morphology, material properties and cytocompatibility. The interdisciplinary """"""""molecular to materials"""""""" design and properties characterization of the proposed hydrogelation system will be accomplished via close collaboration between the chemistry/biochemistry and materials science and engineering departments. This research effort will: 1. Gain a fundamental understanding of the folding and self-assembly process leading to hydrogel formation and how molecular design affects material properties. 2. Enhance the processibility of hairpin-based hydrogels by designing active intramolecular folding triggers that allow peptide solutions to undergo hydrogelation on cue. 3. Determine how peptide structure and material properties affect the adhesion and proliferation of model fibroblast and osteoblast cell lines.

National Institute of Health (NIH)
National Institute of Dental & Craniofacial Research (NIDCR)
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Special Emphasis Panel (ZRG1-BMBI (01))
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Drummond, James
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University of Delaware
Schools of Arts and Sciences
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Sun, Jessie E P; Stewart, Brandon; Litan, Alisa et al. (2016) Sustained release of active chemotherapeutics from injectable-solid ?-hairpin peptide hydrogel. Biomater Sci 4:839-48
Sathaye, Sameer; Mbi, Armstrong; Sonmez, Cem et al. (2015) Rheology of peptide- and protein-based physical hydrogels: are everyday measurements just scratching the surface? Wiley Interdiscip Rev Nanomed Nanobiotechnol 7:34-68
Yan, Congqi; Mackay, Michael E; Czymmek, Kirk et al. (2012) Injectable solid peptide hydrogel as a cell carrier: effects of shear flow on hydrogels and cell payload. Langmuir 28:6076-87
Branco, Monica C; Pochan, Darrin J; Wagner, Norman J et al. (2010) The effect of protein structure on their controlled release from an injectable peptide hydrogel. Biomaterials 31:9527-34
Altunbas, Aysegul; Sharma, Nikhil; Lamm, Matthew S et al. (2010) Peptide--silica hybrid networks: biomimetic control of network mechanical behavior. ACS Nano 4:181-8
Gungormus, Mustafa; Branco, Monica; Fong, Hanson et al. (2010) Self assembled bi-functional peptide hydrogels with biomineralization-directing peptides. Biomaterials 31:7266-74
Yan, Congqi; Altunbas, Aysegul; Yucel, Tuna et al. (2010) Injectable solid hydrogel: mechanism of shear-thinning and immediate recovery of injectable ?-hairpin peptide hydrogels. Soft Matter 6:5143-5156
Branco, Monica C; Schneider, Joel P (2009) Self-assembling materials for therapeutic delivery. Acta Biomater 5:817-31
Branco, Monica C; Pochan, Darrin J; Wagner, Norman J et al. (2009) Macromolecular diffusion and release from self-assembled beta-hairpin peptide hydrogels. Biomaterials 30:1339-47
Branco, Monica C; Nettesheim, Florian; Pochan, Darrin J et al. (2009) Fast dynamics of semiflexible chain networks of self-assembled peptides. Biomacromolecules 10:1374-80

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