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Collagen-based biomaterials have received considerable attention for smarter biomedical applications due to their inherent superior mechano-biological properties. However, accumulating evidence suggests that water, as a probe liquid bound in collagen, might be investigated to explore the influence of additives on the static and dynamic solvation behavior of collagen. The structure and dynamics of water near the surface/interface of collagen-fenugreek composites were demonstrated via circular dichroic spectroscopy, thermoporometry and impedimetric measurements to enlighten about the configuration-function relationship of collagen. Thermodynamic parameters of the composites signify the fenugreek concentration dependent structural robustness of collagen. Thermodynamic parameters such as free energies for unfolding, enthalpies, entropies and activation energies indicate that the residual structure modulates the stability of the denatured state up to 22 kcal mol(-1) and the parameters correlate with structural data for collagen complexed with fenugreek. The association constant of fenugreek is found to be 0.5807 M(-1). The binding of fenugreek influences rearrangement of the collagen-water network, resulting in the transition from a disordered (high entropy) unbound state to a structured (lower entropy) bound state. Fenugreek concentration plays a crucial role in shaping up the free energy that governs the folding, structure and stability of collagen. Dielectric data emphasize the effect of hydrophobic and hydrophilic clusters on the side chain motion constraints. The thermoporometry technique probes the pore size distributions of the composites. These methods provide insights into the role of excluded volume, chain stiffness and stability of a new collagen-galactomannan based composite, expanding its utility in "smart biomaterial applications".