Peptide amphiphiles as supramolecular organisers to engineer fibrinogen into novel fibrin materials
Publication Date
December 12, 2025
Creator
Abstract
Fibrin, the insoluble protein matrix formed during blood coagulation, plays a pivotal role in wound healing and tissue regeneration, not only by providing mechanical support but also through its ability to bind growth factors. Due to its dynamic properties, it regulates key processes such as cell migration, proliferation and extra-cellular matrix deposition.
Peptide amphiphiles (PAs) have already been shown to interact with proteins and complex fluid (e.g. blood), building PA-hydrogels with hierarchically ordered morphologies. The purpose of this study is to present an innovative approach utilising PAs as supramolecular organisers to develop novel fibrinogen-PA co-assembled systems (FibPAs). Specifically, PA-E3 (C15H31CONH-VVVAAAEEE-CONH2) and PA-E3Q (C15H31CONH-VVVAAAEEEQ-CONH2) form FibPAs (FibE3 and FibE3Q, respectively), which preserve the intrinsic functionality of fibrinogen. It results in engineered fibrin oligomers able to polymerise into novel fibrin-based materials with enhanced bio-instructive properties.
Consequently, FibE3 and FibE3Q do not form PA-based hydrogels but guide the physiological process of fibrinogen polymerisation into hierarchically organised structures, characterised by enhanced TGF-β1, VEGF, TNF-α and IL-10 binding. These networks support bone marrow derived mesenchymal stem cells (BM-MSCs) culture and direct their paracrine signalling towards increased pro-angiogenic potential, and enhanced TGF-β1 release.
In conclusion, this innovative approach leverages on supramolecular interactions to control the structure and bioactivity of fibrin networks. The interplay between PAs and fibrinogen opens new possibilities for the bottom-up engineering of functional dynamic biomaterials, showing promising applications in the development of cell-instructive matrices with applicability spanning form regenerative medicine to cell therapies.
Item Type
ethesis
Thesis Type
PhD
Supervisors
Subjects (LC)
Associated Schools / Departments
School of Pharmacy (UK)
eprints ID
81672
UoN Repository URI
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PhD Thesis_Domenico Laurenza (print).pdf
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Full-text
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