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Solution Structural Determination and Dynamics Investigation of BAM8-22 and Truncated Peptides of BAM8-22 by NMR Spectroscopy and Molecular Dynamics Simulation

Author: LvGuoHua
Tutor: DongShouLiang
School: Lanzhou University
Course: Biochemistry and Molecular Biology
Keywords: BAM8-22 Mrg receptor/SNSRs 2D NMR MD simulation Conformation-activity relationship
CLC: Q51
Type: Master's thesis
Year: 2009
Downloads: 3
Quote: 0
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Abstract


Objective: To shed first light on the structural information of Bovine adrenal medullary peptide BAM8-22 (Val-Gly-Arg-Pro-Glu-Trp-Trp-Met-Asp-Tyr-Gln-Lys-Arg-Tyr- Gly), and to gain more detail insight into conformation-activity relationship of BAM8-22 and its truncated peptides on the basis of available function activity study. Methods: The solution structure of BAM8-22 was determined by 2D NMR in water. The dynamic features of BAM8-22 were further investigated by molecular dynamics simulation for 20 ns. Furthermore, the solution structure of BAM8-22 was used to study the conformation characterization of truncated peptide BAM13-22, BAM15-22, BAM8-18 and BAM8-20 by molecular dynamics simulation for 20 ns.Results: BAM8-22 possesses a relatively well-definedα-helix structure during approximately BAM12-20 in aqueous solution, whereas the both termini show highly flexibility. Theα-helix structure of BAM13-22, BAM8-18 and BAM8-20 were spanning from BAM15-20, BAM12-16 and BAM12-18, respectively, while theα-helix structure in BAM15-22 was completely disappeared. Conclusion: From the three-dimentional structure and dynamics features of BAM8-22 and conformational characterization of its truncated peptides, combined with the available functional activity data, it seems reasonable to conclude that the well-definedα-helix structure plays an essential role on the bioactivcity of BAM8-22. All the biophysical data obtained in the current work provides important structural fundation of BAM8-22 which would be helpful to rationally design its analogues and also could be uesd as structural model for further studying its interaction with Mrg receptors.

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CLC: > Biological Sciences > Biochemistry > Protein
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