JKMRS Volume 24, No 4, pp 136, The Structural Studies of Biomi... | |
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2020년 12월 20일 / 조회수: 600 | |
The Structural Studies of
Biomimetic Peptides P99 Derived from Apo B-100 by
NMR
Gil-Hoon Kim, Ho-Shik Won*
Department of Chemistry and Molecular Engineering,
Hanyang University, Ansan 15588, Republic of Korea
Received Dec 10, 2020; Revised
Dec 17, 2020; Accepted Dec 18, 2020
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.
Keywords Apolipoprotein B-100, Immunoglobulin, Molecular dynamic computation, NMR
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첨부파일 | 06-JKMRS_KimGH.pdf |