Solution State Structure of P1, the Mimetic Peptide Derived from IgM Antigen Apo B-100 by NMR

Title
Solution State Structure of P1, the Mimetic Peptide Derived from IgM Antigen Apo B-100 by NMR
Author
원호식
Keywords
Apolipoprotein B-100; Immunoglobulin; Molecular dynamic computation; NMR
Issue Date
2016-09
Publisher
한국자기공명학회
Citation
Journal of the Korean Magnetic Resonance Society, v. 20, No. 3, Page. 95-101
Abstract
Apolipoprotein B-100 (Apo-B100) is a major component of low density lipoprotein (LDL). Apo B-100 protein has 4,536 amino acid sequence and these amino acids are classified into peptide groups A to G with subsequent 20 amino acids (P1-P302). The peptide groups were act as immunoglobulin (Ig) antigens which oxidized via malondialdehyde (MDA). The mimetic peptide P1 (EEEMLENVSLVCPKDAT RFK) out of D-group peptides carrying the highest value of IgG antigens were selected for structural studies that may provide antigen specificity. Circular Dichroism (CD) spectra were measured for peptide secondary structure in the range of 190-250 nm. Ex-perimental results show that P1 exhibit partial of β-sheet and random coil structure. Homonuclear (COSY, TOCSY, NOESY) 2D- NMR experiments were carried out for NMR signal assignments and structure determination for P1. On the basis of these completely assigned NMR spectra and distance data, distance geometry (DG) and Molecular dynamics (MD) were carried out to determine the structures of P1. The proposed structure was selected by comparisons between experimental NOE spectra and back calculated 2D NOE results from determined structure showing acceptable agreement. The total Root-Mean-Square-Deviation (RMSD) value of P1 obtained upon superposition of all atoms was in the range 0.33Å. The solution state P1 has mixed structure of β-sheet (Glu[1] to Cys[12]) and random coil (Pro[13] to Lys[20]). These NMR results are well consistent with secondary structure from ex-perimental results of circular dichroism. Structural studies based on NMR may contribute to the studies of atherosclerosis and observed conformational characteristics of apo B-100 in LDL using monoclo-nal antibodies.
URI
https://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART002144611http://repository.hanyang.ac.kr/handle/20.500.11754/102717
ISSN
1226-6531
DOI
10.6564/JKMRS.2016.20.3.095
Appears in Collections:
COLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY[E](과학기술융합대학) > CHEMICAL AND MOLECULAR ENGINEERING(화학분자공학과) > Articles
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