Dataset Information

β-sheets in serum protein are independent risk factors for coronary lesions besides LDL-C in coronary heart disease patients.

ABSTRACT:

Background

Coronary heart disease (CHD) patients with standard low-density lipoprotein cholesterol (LDL-C) remain at risk of cardiovascular events, making it critical to explore new targets to reduce the residual risk. The relationship between β-sheet conformation and CHD is gaining attention. This study was designed to compare the coronary lesions in CHD patients with varying LDL-C and evaluate whether serum β-sheets are associated with coronary damage.

Methods

Two hundred and one patients diagnosed with stable CHD were recruited and divided into four groups according to LDL-C. Baseline information, coronary lesion-related indicators, and peripheral blood samples were collected. Serum β-sheet content was determined by thioflavin T fluorescence.

Results

The baseline information was comparable in CHD patients with different LDL-C. No difference was found in indicators relevant to coronary lesions among groups. The content of β-sheet was negatively correlated with LDL-C. Multiple linear regression revealed that serum β-sheet was positively correlated with coronary lesion when risk factors such as age, smoking, and LDL-C were controlled.

Conclusions

This is the first study that reports the serum β-sheet levels of CHD patients being gradually increased with decreasing LDL-C when coronary lesions were comparable. Serum β-sheet might exacerbate the coronary lesions in CHD patients independent of known risk factors such as LDL-C.

SUBMITTER: Li YL

PROVIDER: S-EPMC9395970 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature

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Publications

β-sheets in serum protein are independent risk factors for coronary lesions besides LDL-C in coronary heart disease patients.

Li Yu-Lin YL Xie Jia-Ying JY Lu Bin B Sun Xiao-di XD Chen Fang-Fang FF Tong Zhou-Jie ZJ Sai Wen-Wen WW Zhang Wei W Wang Zhi-Hao ZH Zhong Ming M

Frontiers in cardiovascular medicine 20220809

<h4>Background</h4>Coronary heart disease (CHD) patients with standard low-density lipoprotein cholesterol (LDL-C) remain at risk of cardiovascular events, making it critical to explore new targets to reduce the residual risk. The relationship between β-sheet conformation and CHD is gaining attention. This study was designed to compare the coronary lesions in CHD patients with varying LDL-C and evaluate whether serum β-sheets are associated with coronary damage.<h4>Methods</h4>Two hundred and on ...[more]

PMID: 36017095

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Project description:The development of peptide beta-hairpins is problematic, because folding depends on the amino acid sequence and changes to the sequence can significantly decrease folding. Robust beta-hairpins that can tolerate such changes are attractive tools for studying interactions involving protein beta-sheets and developing inhibitors of these interactions. This paper introduces a new class of peptide models of protein beta-sheets that addresses the problem of separating folding from the sequence. These model beta-sheets are macrocyclic peptides that fold in water to present a pentapeptide beta-strand along one edge; the other edge contains the tripeptide beta-strand mimic Hao [JACS 2000, 122, 7654] and two additional amino acids. The pentapeptide and Hao-containing peptide strands are connected by two delta-linked ornithine (deltaOrn) turns [JACS 2003, 125, 876]. Each deltaOrn turn contains a free alpha-amino group that permits the linking of individual modules to form divalent beta-sheets. These "cyclic modular beta-sheets" are synthesized by standard solid-phase peptide synthesis of a linear precursor followed by solution-phase cyclization. Eight cyclic modular beta-sheets 1a-1h containing sequences based on beta-amyloid and macrophage inflammatory protein 2 were synthesized and characterized by 1H NMR. Linked cyclic modular beta-sheet 2, which contains two modules of 1b, was also synthesized and characterized. 1H NMR studies show downfield alpha-proton chemical shifts, deltaOrn delta-proton magnetic anisotropy, and NOE cross-peaks that establish all compounds but 1c and 1g to be moderately or well folded into a conformation that resembles a beta-sheet. Pulsed-field gradient NMR diffusion experiments show little or no self-association at low (</=2 mM) concentrations. Changes to the residues in the Hao-containing strands of 1c and 1g improve folding and show that folding of the structures can be enhanced without altering the sequence of the pentapeptide strand. Well-folded cyclic modular beta-sheets 1a, 1b, and 1f each have a phenylalanine directly across from Hao, suggesting that cyclic modular beta-sheets containing aromatic residues across from Hao are better folded.

Dataset Information

β-sheets in serum protein are independent risk factors for coronary lesions besides LDL-C in coronary heart disease patients.

Background

Methods

Results

Conclusions

Publications

β-sheets in serum protein are independent risk factors for coronary lesions besides LDL-C in coronary heart disease patients.

Similar Datasets

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