Water Dynamics in Egg White Peptide, Asp-His-Thr-Lys-Glu, Powder Monitored by Dynamic Vapor Sorption and LF-NMR.
Water absorbed into the bulk amorphous structure of peptides can have profound effects on their properties. Here, we elucidated water dynamics in Asp-His-Thr-Lys-Glu (DHTKE), an antioxidant peptide derived from egg white ovalbumin, using water dynamic vapor sorption (DVS) and low-field nuclear magnetic resonance (LF-NMR). The DVS results indicated that parallel exponential kinetics model fitted well to the data of sorption kinetics behavior of DHTKE. Four different proton fractions with different mobilities were identified based on the degree of interaction between peptide and water. The water could significantly change the proton distribution and structure of the sample. The different phases of moisture absorption were reflected in the T2 parameters. In addition, the combined water content was dominant in the hygroscopicity of DHTKE. This study provides an effective real-time monitoring method for water mobility and distribution in synthetic peptides, and this method may have applications in promoting peptide quality assurance.
['Yang|Shuailing|S|', 'Liu|Xuye|X|', 'Jin|Yan|Y|', 'Li|Xingfang|X|', 'Chen|Feng|F|', 'Zhang|Mingdi|M|', 'Lin|Songyi|S|']
D000818:Animals D002645:Chickens D004529:Egg White D007700:Kinetics D009682:Magnetic Resonance Spectroscopy D010455:Peptides D013227:Steam D014867:Water
egg white peptide dynamic vapor sorption LF-NMR moisture absorption water distribution