caa a22 4500 445326360 CHVBK 20180317142722.0 cr unu---uuuuu 170323e20110301xx s 000 0 eng 10.1007/s10989-011-9241-4 doi (NATIONALLICENCE)springer-10.1007/s10989-011-9241-4 Comparison of Non-covalent Interactions Between a Series of N -Phosphoryl Dipeptide or Methyl Esters and Protein by Electrospray Ionization Mass Spectrometry [Elektronische Daten] [Li-ming Qiang, Ming-xiu Lü, Xu-ru Dong, Shu-xia Cao, Kui Lu, Yu-fen Zhao] The non-covalent interaction between a series of N-phosphoryl dipeptides (or methyl esters) (DPP) and protein was studied by ESI-MS and UV-vis spectrometer. The function of different groups in DPP and binding sites of protein were investigated. The results revealed that hydroxyl and aromatic ring in DPP were both important group for the interaction, and aromatic ring had double functions on the interaction. In addition, the molecular size, flexibility and steric hindrance showed obvious effects on the interaction, while, the chirality, sequence and length of carbon chains (changing 1-2C) of amino acid residue in DPP showed little effects on the interaction under the experimental conditions. Phosphoryl oligopeptides having extended structure, good molecular flexibility and smaller spatial hindrance could contract the protein conformation in solution. The aromatic, basic, acid and amide amino acid residues of protein may be the main binding sites and contributed to the survival of the complexes. Springer Science+Business Media, LLC, 2011 N -phosphoryl dipeptide (or methyl esters) nationallicence Noncovalent weak interaction nationallicence Cytochrome C nationallicence Bovine serum albumin nationallicence ESI-MS nationallicence Qiang Li-ming Department of Chemistry, Zhengzhou University, 450052, Zhengzhou, China aut Lü Ming-xiu Department of Material and Chemical Engineering, Henan Institute of Engineering, 450007, Zhengzhou, China aut Dong Xu-ru Department of Material and Chemical Engineering, Henan Institute of Engineering, 450007, Zhengzhou, China aut Cao Shu-xia Department of Chemistry, Zhengzhou University, 450052, Zhengzhou, China aut Lu Kui Department of Material and Chemical Engineering, Henan Institute of Engineering, 450007, Zhengzhou, China aut Zhao Yu-fen Department of Chemistry, Zhengzhou University, 450052, Zhengzhou, China aut International Journal of Peptide Research and Therapeutics Springer Netherlands 17/1(2011-03-01), 61-67 1573-3149 17:1<61 2011 17 10989 https://doi.org/10.1007/s10989-011-9241-4 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10989-011-9241-4 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Qiang Li-ming Department of Chemistry, Zhengzhou University, 450052, Zhengzhou, China aut NATIONALLICENCE 700 1- Lü Ming-xiu Department of Material and Chemical Engineering, Henan Institute of Engineering, 450007, Zhengzhou, China aut NATIONALLICENCE 700 1- Dong Xu-ru Department of Material and Chemical Engineering, Henan Institute of Engineering, 450007, Zhengzhou, China aut NATIONALLICENCE 700 1- Cao Shu-xia Department of Chemistry, Zhengzhou University, 450052, Zhengzhou, China aut NATIONALLICENCE 700 1- Lu Kui Department of Material and Chemical Engineering, Henan Institute of Engineering, 450007, Zhengzhou, China aut NATIONALLICENCE 700 1- Zhao Yu-fen Department of Chemistry, Zhengzhou University, 450052, Zhengzhou, China aut NATIONALLICENCE 773 0- International Journal of Peptide Research and Therapeutics Springer Netherlands 17/1(2011-03-01), 61-67 1573-3149 17:1<61 2011 17 10989 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer