Citation:
CHEN Chen, CHU Yan-Qiu, DAI Xin-Hua, FANG Xiang, DING Chuan-Fan. Investigation of the Non-Covalent Interactions between Fragment Peptides of Bradykinin by Mass Spectrometry[J]. Acta Physico-Chimica Sinica,
;2013, 29(06): 1336-1343.
doi:
10.3866/PKU.WHXB201303155
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To explore the important factors affecting the stability of gas phase bradykinin (R1P2P3G4F5S6P7F8R9), the non-covalent interactions between fragment peptides of bradykinin were investigated by electrospray ionization mass spectrometry (ESI-MS). The fracture sites are S6P7 (mode 1) and F5S6 (mode 2). The fragment peptides of bradykinin and its des-arginine analogues were synthesized. ESI-MS results showed that the fragment peptides of bradykinin obtained in the two modes can easily react by non-covalent interactions. In fracture mode 1, when R9 was removed, the peptide PF seldom bound to any other fragment peptide. While in fracture mode 2, non-covalent binding still occurred between fragment peptides when either R1 or R9 was removed, which indicates that serine is likely to be at the position of the β-turn. The collision induced dissociation (CID) revealed that the binding strength between RPPGFS and PFR, or RPPGF and SPFR, is stronger than for the peptides without R. For the complexes of RPPGFS with PFR, and RPPGF with SPFR, the binding constant (Kst) values determined by mass spectrometric titrations were 3.53×103 and 3.16×103, respectively, which are greater than the Kst value (1.25×103) of the complexes of PPGF with SPF. The mass spectrometric titrations confirmed the results from CID, indicating that the hydrogen bonds between the arginine residues of the two terminals of bradykinin play an important role in stabilizing the conformation of gas phase bradykinin.
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