Bijaylaxmi Patra (Centre of BioMedical Research (CBMR), India)
LinkedIn: @Bijaylaxmi Patra; X: @BijaylaxmiNMR; Bluesky: @bijaylaxmi.bsky.social
Abstract: Collagen, the most abundant protein in animals, is a major structural constituent of muscle and connective tissues and plays a crucial role in determining their mechanical properties. Its structure and stability are strongly influenced by interactions with the surrounding environment, particularly water; however, the molecular basis of these effects remains insufficiently understood. In this study, we probe dehydration–induced changes in collagen dynamics within the native bone extracellular matrix (ECM) using 13C solid–state Nuclear Magnetic Resonance (NMR) relaxation measurements (T1 and T2) along with rotational correlation time analysis to examine water–collagen interactions at the molecular level. Our residue–specific investigation uncovers distinct motional behavior among the aliphatic carbons of the Gly–Pro–Hyp triplet and alanine residues, which together account for nearly 70% of type I collagen. The extracted 13C correlation times reveal substantial motional heterogeneity, where dehydration primarily suppresses the mobility of hydroxyproline Cβ, while H/D exchange significantly affects hydroxyproline Cα, Cβ, and Cγ, as well as glycine Cα. These results provide new insights into hydration–dependent collagen dynamics in native bone and demonstrate the utility of 13C relaxation measurements for investigating water–mediated stabilization and motion in collagen, with broader implications for understanding pathological processes and designing biomimetic materials.
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