ABSTRACT
The structure of water, especially around the solute is thought to play an important role in many biological and chemical processes. Water-peptide and cosolvent-peptide interactions are crucial in determining the structure and function of protein molecules. In this work, we present the H-bonding analysis for model peptides like glycyl-glycine (gly-gly), glycine-Ö-valine (gly-val), glycyl-Ö-leucine (gly-leu) and triglycine (trigly) and triethylammonium based carboxylate protic ionic liquids (PILs) in aqueous solutions as well as for peptides in â¼0.2 mol·L-1 of aqueous PIL solutions in the spectral range of 7800-5500 cm-1 using Fourier transform near-infrared (FT-NIR) spectroscopy at 298.15 K. The hydration numbers for peptides and PILs were obtained using NIR method of simultaneous estimation of hydration spectrum and hydration number of a solute dissolved in water. The H-bond of water molecules around peptides and PILs are found to be stronger and shorter than those in pure liquid water. We observe that the hydration shell around zwitterions is a clathrate-like cluster of water in which ions entrap. Watery network analysis confirms that singly H-bonded species or NHBs changes to partial or distorted ice-like structures of water in the hydration shell of PILs. The overall water H-bonding in the hydration sphere of PILs increases in the order TEAF < TEAA < TEAG < TEAPy ≈ TEAP < TEAB. The influence of PILs on hydration behavior of peptides is explored in terms of H-bonding, cooperativity, hydrophobicity, water structural changes, ionic interactions etc.