150 0

The Structural Studies of Biomimetic Peptides P99 Derived from Apo B-100 by NMR

Title
The Structural Studies of Biomimetic Peptides P99 Derived from Apo B-100 by NMR
Author
원호식
Keywords
Apolipoprotein B-100; Immunoglobulin; Molecular dynamic computation; NMR
Issue Date
2020-12
Publisher
한국자기공명학회
Citation
Journal of the Korean Magnetic Resonance Society, v. 24, no. 4, page. 136-142
Abstract
Apolipoprotein B-100 (apo B-100), the main protein component that makes up LDL (Low density lipoprotein), consists of 4,536 amino acids and serves to combine with the LDL receptor. The oxidized LDL peptides by malondialdehyde (MDA) or acetylation in vivo were act as immunoglobulin (Ig) antigens and peptide groups were classified into 7 peptide groups with subsequent 20 amino acids (P1-P302). The biomimetic peptide P99 (KGTYG LSCQR DPNTG RLNGE) out of B-group peptides carrying the highest value of IgM 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 190-260 nm. Experimental results show that P99 has pseudo α-helice and random coil structure. Homonuclear (COSY, TOCSY, NOESY) 2D-NMR experiments were carried out for NMR signal assignments and structure determination for P99. On the basis of these completely assigned NMR spectra and proton distance information, distance geometry (DG) and molecular dynamic (MD) were carried out to determine the structures of P99. 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 P99 obtained upon superposition of all atoms were in the set range. The solution state P99 has mixed structure of pseudo α-helix and β-turn(Gln[9] to Thr[13]). These NMR results are well consistent with secondary structure from experimental results of circular dichroism. Structural studies based on NMR may contribute to the prevent oxidation studies of atherosclerosis and observed conformational characteristics of apo B-100 in LDL using monoclonal antibodies.
URI
https://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART002657603https://repository.hanyang.ac.kr/handle/20.500.11754/164992
ISSN
1226-6531
DOI
10.6564/JKMRS.2020.24.4.136
Appears in Collections:
COLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY[E](과학기술융합대학) > CHEMICAL AND MOLECULAR ENGINEERING(화학분자공학과) > Articles
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE