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Details of Grant 

EPSRC Reference: EP/R011818/1
Title: Collagen assembly: from molecules to fibrils
Principal Investigator: Saric, Dr A
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Department: Physics and Astronomy
Organisation: UCL
Scheme: First Grant - Revised 2009
Starts: 28 March 2018 Ends: 29 February 2020 Value (£): 100,772
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No relevance to Underpinning Sectors
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Panel History:
Panel DatePanel NameOutcome
13 Sep 2017 EPSRC Physical Sciences - September 2017 Announced
Summary on Grant Application Form
One of the most remarkable examples of self-assembly in living organisms is the formation of collagen architectures. Collagen is the most abundant protein in the animal kingdom, where its molecules robustly self-associate into micron-sized fibrils of well defined morphologies. These fibrils form the structural basis of mammalian connective tissues and, as the major component of the extracellular matrix, are crucial for the determination of cell phenotype, cell adhesion, and tissue regulation and signalling. For the same reasons the process of collagen assembly is also at the centre of engineering efforts to design functional biomimetic materials and platforms for cell and tissue manipulation. However, the current understanding of the physical processes that drive collagen assembly from molecules to micron-sized fibrils, and the determinants of the resulting morphologies, is far from complete.

The goals of this project are to bridge molecular and microscopic scales of the dynamic process of collagen assembly, and identify the physical principles of the assembly of collagen and collagen-mimetic molecules. This will be achieved by developing a minimal physical model of collagen-like molecules, implemented in a molecular dynamics framework. Because of its simplicity, such a physical model can reach experimentally relevant time- and length-scales of the assembly, and its results can be directly compared with experiments of our collaborators. Two specific objectives are to: 1) Map the design of small collagen-mimetic molecules on the resulting fibrillar architectures, and hierarchical pathways of fibril nucleation and growth. 2) Investigate the influence of the molecular charge patterns and hydrophobic interactions on the self-assembly of native collagen molecules. The long-term goals are to understand the physical principles behind robust collagen assembly in nature, as well as the roots of its failure in pathological processes, and to provide guidelines for the rational design of collagen-mimetic materials. The results from this project will give insights into the roots of collagen remodelling in diseases and ageing, and guide the design of collagen scaffolds for biotechnological applications.
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