Polyethyleneglycol–pepsin interaction and its relationship with protein partitioning in aqueous two-phase systems |
| |
| Institution: | 1. Physical Chemistry Department, Faculty of Biochemical and Pharmaceutical Sciences, CONICET, FonCyT and CIUNR, National University of Rosario, Suipacha 570, S2002RLK Rosario, Argentina;2. Applied Physics Department, Faculty of Sciences Campus Ourense, University of Vigo, As Lagoas s/n, E-32004 Ourense, Spain;1. Institute of Analytical Chemistry for Life Science, Nantong University, Nantong 226019, China;2. School of Public Health, Nantong University, Nantong 226019, China;3. Affiliated Hospital, Nantong University, Nantong 226021, China;1. University of Jyvaskyla, Department of Physics and Nanoscience Center, P.O. Box 35, FI-40014 University of Jyvaskyla, Finland;2. CIRIMAT, Université de Toulouse, CNRS, INPT, UPS, UMR CNRS-UPS-INP No. 5085, Université Toulouse 3 Paul Sabatier, Bât. CIRIMAT, 118, route de Narbonne, 31062 Toulouse Cedex 9, France;1. Department of Medical Parasitology & Mycology, The School of Medicine, Yazd Shahid Sadoughi University of Medical Sciences, Yazd, Iran;2. Department of Laboratory Sciences, School of Paramedicine, Shahid Sadoughi University of Medical Sciences, Yazd, Iran;3. Reproductive Immunology Research Center, Shahid Sadoughi University of Medical Sciences, Yazd, Iran;4. Department of Medical Nanotechnology, Pajoohesh Lab, Yazd, Iran;1. Institute of Super-Microstructure and Ultrafast Process in Advanced Materials & Hunan Key Laboratory for Super-microstructure and Ultrafast Process, School of Physics and Electronics, Central South University, Changsha 410083, China;2. School of Materials Science and Engineering, Central South University, Changsha 410083, China;3. Department of Applied Physics, Hunan University, Changsha 410082, China |
| |
| Abstract: | The interaction between the acidic protein, pepsin, and the non-charged polyethyleneglycol polymer was studied by dynamic light scattering, fluorescence spectroscopy and measurements of the protein thermal stability at neutral pH. Polyethyleneglycol of average molecular mass 1450 showed a higher interaction capacity with the protein than polyethyleneglycol of average molecular mass 8000. Polyethyleneglycol of average molecular mass 1450 showed a molecular mechanism where the interpolymer interaction led to the complex formation. This fact can be explained taking into account that the extended form on this polymer molecule favours the interaction with the protein, which is highly dependent of the polymer total concentration. Polyethyleneglycol of average molecular mass 8000 showed a cooperative interaction between the polymer and protein molecules which was independent of the PEG concentration. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
