| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1428216 | Materials Science and Engineering: C | 2015 | 7 Pages |
•Hydration state of gelatin is evaluated by differential scanning calorimetry.•Polycaprolactone affects hydration shell of gelatin by diverse H-bond formation.•Reorientation of H-bond plays a crucial role in drug delivery.
Dynamic properties of water molecules present in the vicinity of protein are sensitive to its local conformational motions. Water mobility at the protein surface/interfaces is affected by its polar and charged groups, which are capable of anchoring water molecules through H-bonds. Differential scanning calorimetry, ATR–FTIR spectroscopy and circular dichroic analysis have been employed to substantiate the changes in hydration of gelatin, interacting with polycaprolactone. Enthalpy of denaturation and decrease in melting temperature indicate alteration in water-bridges around gelatin. In vitro drug release studies substantiate the influence of hydration on its release kinetics. These studies would aid in exploration of potential drug carrier.
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