Efficient utilisation of lower value meat is a challenge, in particular its extraction and conversion to an edible food product. In animal muscle tissue, type I collagen is the most abundant protein and of all the proteins present in muscle, collagen affects meat tenderness the most and is the focus of this study. Collagen is comprised of three polypeptide chains, which form a triple helical structure. The three polypeptide chains consist of two imino acids, proline and hydroxyproline, which occur in a common triad repeat POG or GPO, (where P=proline, O=hydroxyproline and G=glycine). Triple helices further self-assemble into high order fibers.  Self-assembly is a naturally occurring process in collagen. Understanding how this assembly takes place, and how it can be controlled, is the aim of my research. Our hypothesis that oxidative modifications impact on the assembly of the collagen helix and ultimately the texture of collagen containing foods. The reason that oxidative modifications have been taken into account is that during meat processing, e.g. cooking, (which is a kind of heat treatment capable of bringing oxidations) there is production of reactive oxygen species (ROS) and these are highly likely to play a significant role in modification to meat properties associated with cooking. For example, hydroxylation of proline will increase the overall content of hydroxyproline, which will likely result in changes to protein self- assembly and self-association. These types of changes in collagen will be studied.

Collagen peptides have been selected based on (1) the increment of number of residues and (2) replacement of residues by modified residues (such as oxidised ones). In solution studies, triple helix formation as the 1st step of self assembly has been confirmed for all the selected collagen mimetic peptides by CD and DSC experiments. The melting temperature and enthalpy of melting for different peptides have been measured (DSC) to check the strength and stability of triple helix at various conditions of temperature, buffers, and incubation times. These above mentioned heating experiments are the melting studies of the selected peptides carried out by DSC and CD to check the unwinding and rewinding of helices.

Crystallisation of peptides is being carried out, successfully crystallising 4 peptides, where two peptide crystals have diffracted and one has been solved till date.