Yanli Liang

Publications (2)5.47 Total impact

• Article: Separation of peptides with an aqueous mobile phase by temperature-responsive chromatographic column (J. Sep. Science 35'16).

  Rongji Dai, Zongjian Liu, Yanli Liang, Fangfang Geng, Chen Ge, Kaleem Ullah, Fang Lv, Yukui Zhang, Yulin Deng
  [show abstract] [hide abstract]
  ABSTRACT: DOI: 10.1002/jssc.201200247 A thermoresponsive chromatographic material was prepared through a simple method and employed for the temperature-modulated separation of peptides in an aqueous mobile phase. At 10°C, the grafted polymer chains are hydrophilic and in the form of extended coil. In this case, the peptides were unable to be separated and showed a single peak in chromatograms. In contrast, the polymer is hydrophobic and in the form of collapsed globule at 50°C. In this case, the peptides were completely separated because of the enhanced hydrophobic interaction of peptides and stationary phase.
  Journal of Separation Science 08/2012; 35(16):NA. · 2.73 Impact Factor
• Article: Separation of peptides with an aqueous mobile phase by temperature-responsive chromatographic column.

  Zongjian Liu, Yanli Liang, Fangfang Geng, Chen Ge, Kaleem Ullah, Fang Lv, Rongji Dai, Yukui Zhang, Yulin Deng
  [show abstract] [hide abstract]
  ABSTRACT: Peptide separation technology is significant and is still an analytical challenge in proteomic studies. We report a simple preparation method for poly(N-isopropylacrylamide) grafted silica through the copolymerization of N-isopropylacrylamide with acetyl moieties immobilized on the silica surfaces. Differential scanning calorimetry results indicated that the prepared silica exhibited a sharp phase transition at 35.03°C. Silica grafted with poly(N-isopropylacrylamide) was evaluated as a temperature-responsive chromatography medium for the separation of peptides using 0.2 M NaCl solution as a mobile phase. Results indicated that at 10°C, the peptides were not resolved, but baseline separation with prolonged retention time at 50°C was attained. Particularly, a mixture of four peptides was efficiently separated within 8 min. The theoretical plate number of every peptide was more than 2500, and the resolutions were more than 3.40. The increased selectivity of the temperature-responsive column resulted from the temperature-modulated hydrophobic interaction with peptides. The retention times of these peptides were related to their hydrophobicities. This protocol provided a reliable set of chromatographic tool usable across all research and development applications that required isolation and analysis of peptides. It may represent a step forward in the complex analysis of hydrophobic and other proteins.
  Journal of Separation Science 07/2012; 35(16):2069-74. · 2.73 Impact Factor