Keywords

Non-Covalent Interaction, Bradykinin, Peptide Fragment, Mass Spectrometry, Collision-Induced Dissociation, Binding Constant

Abstract

Taking bradykinin (r1p2p3g4f5s6p7f8r9) molecule as a research model, electrospray mass spectrometry was used to study the non-covalent interactions between bradykinin molecule fragments, and explore the hydrogen bonding interactions that affect the stability of the molecular conformation of the gas phase polypeptide. Synthesized with bradykinin The fragments formed by fragmentation of the peptide molecule at position 1 are consistent with the rppgfs and pfr polypeptide sequences, the rppgf and spfr polypeptides are consistent with the fragments formed by fragmentation at position 2, and the corresponding fragmented polypeptides with arginine removed from the N-terminus or C-terminus. Experimental results show that, The fragmented peptides generated at the above two cleavage positions can have non-covalent interactions after reacting separately. In cleavage mode 1, after removing the arginine r at the C-terminal, the pfr polypeptide does not interact non-covalently with most other peptides. Binding, indicating that r in pfr plays an important role in the conformation of bradykinin gas phase molecules. In fragmentation mode 2, there is non-covalent binding between polypeptides with the N-terminal or C-terminal arginine removed, that is, c Spf or spfr polypeptide fragments with serine at the end can still hydrogen bond with the N-terminal fragment, indicating that serine is likely to be in a corner position. Through collision energy analysis of collision-induced dissociation (cid), it was found that the polypeptides rppgfs and pfr, And the hydrogen bonding between the polypeptides rppgf and spfr is strong, while the hydrogen bonding between the polypeptide obtained by removing the N-terminal and C-terminal arginine at the same time is weak. The binding constant of rppgfs and pfr quantitatively measured by mass spectrometry titration is: 3.53¡Á103, which is close to the binding constants of rppgf and spfr (3.16¡Á103). They are both larger than the binding constants of ppgf and spf (1.25¡Á103) without arginine. The results of mass spectrometry titration experiments further confirmed the collision-induced dissociation. The analysis results show that the hydrogen bonding between the arginines at both ends of the bradykinin molecule is one of the important factors that stabilizes the conformation of the gas-phase bradykinin molecule.

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Original research done by Chen Chen, Chu Yanqiu, Dai Xinhua, Xiang Xiang, Ding Chuanfan

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