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  1. TI=Structure and function of HDL mimetics
  2. AU="Shimoe, Atsuhiro"

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  1. Artikel ; Online: Structure and function of HDL mimetics.

    Navab, Mohamad / Shechter, Ishaiahu / Anantharamaiah, G M / Reddy, Srinivasa T / Van Lenten, Brian J / Fogelman, Alan M

    Arteriosclerosis, thrombosis, and vascular biology

    2009  Band 30, Heft 2, Seite(n) 164–168

    Abstract: HDL mimetics have been constructed from a number of peptides and proteins with varying structures ... with as few as 4 and as many as 243 amino acid residues. Some HDL mimetics have been constructed ... and in early human clinical trials, HDL mimetics appear to have promise as diagnostic and therapeutic ...

    Abstract HDL mimetics have been constructed from a number of peptides and proteins with varying structures, all of which bind lipids found in HDL. HDL mimetics containing a peptide or protein have been constructed with as few as 4 and as many as 243 amino acid residues. Some HDL mimetics have been constructed with lipid but without a peptide or protein component. Some HDL mimetics promote cholesterol efflux, some have been shown to have a remarkable ability to bind oxidized lipids compared to human apolipoprotein A-I (apoA-I). Many of these peptides have been shown to have antiinflammatory properties. Based on studies in a number of animal models and in early human clinical trials, HDL mimetics appear to have promise as diagnostic and therapeutic agents.
    Mesh-Begriff(e) Administration, Oral ; Animals ; Anti-Inflammatory Agents/administration & dosage ; Anti-Inflammatory Agents/chemistry ; Anti-Inflammatory Agents/metabolism ; Anti-Inflammatory Agents/pharmacology ; Apolipoprotein A-I/metabolism ; Cardiovascular Diseases/drug therapy ; Cardiovascular Diseases/metabolism ; Cholesterol/metabolism ; Humans ; Hypolipidemic Agents/administration & dosage ; Hypolipidemic Agents/chemistry ; Hypolipidemic Agents/metabolism ; Hypolipidemic Agents/pharmacology ; Lipoproteins, HDL/chemistry ; Lipoproteins, HDL/metabolism ; Molecular Mimicry ; Oxidation-Reduction ; Peptides/administration & dosage ; Peptides/chemistry ; Peptides/metabolism ; Peptides/pharmacology ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship
    Chemische Substanzen APOA1 protein, human ; Anti-Inflammatory Agents ; Apolipoprotein A-I ; Hypolipidemic Agents ; Lipoproteins, HDL ; Peptides ; Cholesterol (97C5T2UQ7J)
    Sprache Englisch
    Erscheinungsdatum 2009-07-16
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Review
    ZDB-ID 1221433-4
    ISSN 1524-4636 ; 1079-5642
    ISSN (online) 1524-4636
    ISSN 1079-5642
    DOI 10.1161/ATVBAHA.109.187518
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: The structure/function of apoprotein A-I mimetic peptides: an update.

    Getz, Godfrey S / Reardon, Catherine A

    Current opinion in endocrinology, diabetes, and obesity

    2014  Band 21, Heft 2, Seite(n) 129–133

    Abstract: ... from the plasma and HDL and suggests modulation of bioactive oxidized lipids in the intestine by the peptides ... findings: The apoA-I mimetic peptides are based on the structure of the major apoprotein of HDL ... of apoprotein A-I (apoA-I) mimetic peptides and improved methods for the oral delivery of peptides.: Recent ...

    Abstract Purpose of review: To review recent advances in our understanding of the mechanism of action of apoprotein A-I (apoA-I) mimetic peptides and improved methods for the oral delivery of peptides.
    Recent findings: The apoA-I mimetic peptides are based on the structure of the major apoprotein of HDL with the expectation that they may also mimic some of the antiatherogenic functions of HDL. Recent work has provided insight into mechanisms by which they may be antioxidative and anti-inflammatory. In addition, recent work has shifted the focus of the site of action of the mimetic peptides to the small intestine from the plasma and HDL and suggests modulation of bioactive oxidized lipids in the intestine by the peptides may be a major antiatherogenic pathway. The development of transgenic tomatoes expressing an apoA-I mimetic peptide is a significant advance in the oral delivery of peptides as therapies for cardiovascular disease and other chronic inflammatory disorders.
    Summary: In the past year, there have been important advances in the field of apoA-I mimetic peptides, including the oral delivery of bioactive peptides. Further work is required to fully understand the molecular basis for the effect of the peptide on the intestine and bioactive oxidized lipids.
    Mesh-Begriff(e) Anti-Inflammatory Agents/pharmacology ; Antioxidants/chemistry ; Apolipoprotein A-I/chemistry ; Atherosclerosis/immunology ; Atherosclerosis/prevention & control ; Biomimetic Materials/chemistry ; Biomimetic Materials/pharmacology ; Diet ; Female ; Humans ; Inflammation/immunology ; Inflammation/prevention & control ; Intestine, Small/immunology ; Lycopersicon esculentum/genetics ; Lysophospholipids/pharmacology ; Male ; Plants, Genetically Modified/genetics ; Structure-Activity Relationship
    Chemische Substanzen Anti-Inflammatory Agents ; Antioxidants ; Apolipoprotein A-I ; Lysophospholipids ; lysophosphatidic acid (PG6M3969SG)
    Sprache Englisch
    Erscheinungsdatum 2014-04
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2272017-0
    ISSN 1752-2978 ; 1752-296X
    ISSN (online) 1752-2978
    ISSN 1752-296X
    DOI 10.1097/MED.0000000000000045
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Structure/function relationships of apolipoprotein a-I mimetic peptides: implications for antiatherogenic activities of high-density lipoprotein.

    D'Souza, Wilissa / Stonik, John A / Murphy, Andrew / Demosky, Steven J / Sethi, Amar A / Moore, Xiao L / Chin-Dusting, Jaye / Remaley, Alan T / Sviridov, Dmitri

    Circulation research

    2010  Band 107, Heft 2, Seite(n) 217–227

    Abstract: ... functions of HDL may have different mechanisms and different structural requirements. The results do suggest ... functions of HDL is poorly understood.: Objective: To establish structure/function relationships of apoA ... I mimetic peptides with their antiatherogenic functions.: Methods and results: Twenty-two bihelical apoA ...

    Abstract Rationale: Apolipoprotein (apoA)-I mimetic peptides are a promising type of anti-atherosclerosis therapy, but how the structural features of these peptides relate to the multiple antiatherogenic functions of HDL is poorly understood.
    Objective: To establish structure/function relationships of apoA-I mimetic peptides with their antiatherogenic functions.
    Methods and results: Twenty-two bihelical apoA-I mimetic peptides were investigated in vitro for the capacity and specificity of cholesterol efflux, inhibition of inflammatory response of monocytes and endothelial cells, and inhibition of low-density lipoprotein (LDL) oxidation. It was found that mean hydrophobicity, charge, size of hydrophobic face, and angle of the link between the helices are the major factors determining the efficiency and specificity of cholesterol efflux. The peptide with optimal parameters was more effective and specific toward cholesterol efflux than human apoA-I. Charge and size of hydrophobic face were also the major factors affecting antiinflammatory properties, and the presence of cysteine and histidine residues was the main factor determining antioxidant properties. There was no significant correlation between capacities of the peptides to support individual functions; each function had its own optimal set of features.
    Conclusions: None of the peptides was equally effective in all the antiatherogenic functions tested, suggesting that different functions of HDL may have different mechanisms and different structural requirements. The results do suggest, however, that rationalizing the design of apoA-I mimetic peptides may improve their therapeutic value and may lead to a better understanding of mechanisms of various antiatherogenic functions of HDL.
    Mesh-Begriff(e) ATP Binding Cassette Transporter 1 ; ATP-Binding Cassette Transporters/metabolism ; Animals ; Anti-Inflammatory Agents/chemistry ; Anti-Inflammatory Agents/pharmacology ; Antioxidants/chemistry ; Antioxidants/pharmacology ; Apolipoprotein A-I/metabolism ; Atherosclerosis/immunology ; Atherosclerosis/metabolism ; Atherosclerosis/prevention & control ; Biological Transport ; Cardiovascular Agents/chemistry ; Cardiovascular Agents/pharmacology ; Cell Line ; Cholesterol/metabolism ; Drug Design ; Endothelial Cells/drug effects ; Endothelial Cells/immunology ; Endothelial Cells/metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Inflammation Mediators/metabolism ; Lipoproteins, LDL/metabolism ; Mice ; Molecular Mimicry ; Monocytes/drug effects ; Monocytes/immunology ; Monocytes/metabolism ; Peptides/chemistry ; Peptides/pharmacology ; Protein Conformation ; Structure-Activity Relationship ; Surface Properties
    Chemische Substanzen ATP Binding Cassette Transporter 1 ; ATP-Binding Cassette Transporters ; Anti-Inflammatory Agents ; Antioxidants ; Apolipoprotein A-I ; Cardiovascular Agents ; Inflammation Mediators ; Lipoproteins, LDL ; Peptides ; oxidized low density lipoprotein ; Cholesterol (97C5T2UQ7J)
    Sprache Englisch
    Erscheinungsdatum 2010-05-27
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80100-8
    ISSN 1524-4571 ; 0009-7330 ; 0931-6876
    ISSN (online) 1524-4571
    ISSN 0009-7330 ; 0931-6876
    DOI 10.1161/CIRCRESAHA.110.216507
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: High-density lipoprotein in diabetes: Structural and functional relevance.

    Lui, David Tak Wai / Tan, Kathryn Choon Beng

    Journal of diabetes investigation

    2024  

    Abstract: ... into the structure-function relationship of HDL in diabetes. Interestingly, HDL also has a pleiotropic anti-diabetic ... oxidative stress, and systemic inflammation can modify the HDL composition and therefore the functions, especially ... functions rather than to increase HDL-C levels. Among these, recombinant HDL and small synthetic ...

    Abstract Low levels of high-density lipoprotein-cholesterol (HDL-C) is considered a major cardiovascular risk factor. However, recent studies have suggested a more U-shaped association between HDL-C and cardiovascular disease. It has been shown that the cardioprotective effect of HDL is related to the functions of HDL particles rather than their cholesterol content. HDL particles are highly heterogeneous and have multiple functions relevant to cardiometabolic conditions including cholesterol efflux capacity, anti-oxidative, anti-inflammatory, and vasoactive properties. There are quantitative and qualitative changes in HDL as well as functional abnormalities in both type 1 and type 2 diabetes. Non-enzymatic glycation, carbamylation, oxidative stress, and systemic inflammation can modify the HDL composition and therefore the functions, especially in situations of poor glycemic control. Studies of HDL proteomics and lipidomics have provided further insights into the structure-function relationship of HDL in diabetes. Interestingly, HDL also has a pleiotropic anti-diabetic effect, improving glycemic control through improvement in insulin sensitivity and β-cell function. Given the important role of HDL in cardiometabolic health, HDL-based therapeutics are being developed to enhance HDL functions rather than to increase HDL-C levels. Among these, recombinant HDL and small synthetic apolipoprotein A-I mimetic peptides may hold promise for preventing and treating diabetes and cardiovascular disease.
    Sprache Englisch
    Erscheinungsdatum 2024-02-28
    Erscheinungsland Japan
    Dokumenttyp Journal Article ; Review
    ZDB-ID 2625840-7
    ISSN 2040-1124 ; 2040-1116
    ISSN (online) 2040-1124
    ISSN 2040-1116
    DOI 10.1111/jdi.14172
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: A retractable lid in lecithin:cholesterol acyltransferase provides a structural mechanism for activation by apolipoprotein A-I.

    Manthei, Kelly A / Ahn, Joomi / Glukhova, Alisa / Yuan, Wenmin / Larkin, Christopher / Manett, Taylor D / Chang, Louise / Shayman, James A / Axley, Milton J / Schwendeman, Anna / Tesmer, John J G

    The Journal of biological chemistry

    2017  Band 292, Heft 49, Seite(n) 20313–20327

    Abstract: ... by apolipoprotein A-I (apoA-I) and other mimetic peptides that form a belt around HDL. Here, we report the crystal ... lipoproteins (HDL) from discoidal to spherical particles. LCAT is activated through an unknown mechanism ... conformation. Residues Thr-123 and Phe-382 in the catalytic domain form a latch-like ...

    Abstract Lecithin:cholesterol acyltransferase (LCAT) plays a key role in reverse cholesterol transport by transferring an acyl group from phosphatidylcholine to cholesterol, promoting the maturation of high-density lipoproteins (HDL) from discoidal to spherical particles. LCAT is activated through an unknown mechanism by apolipoprotein A-I (apoA-I) and other mimetic peptides that form a belt around HDL. Here, we report the crystal structure of LCAT with an extended lid that blocks access to the active site, consistent with an inactive conformation. Residues Thr-123 and Phe-382 in the catalytic domain form a latch-like interaction with hydrophobic residues in the lid. Because these residues are mutated in genetic disease, lid displacement was hypothesized to be an important feature of apoA-I activation. Functional studies of site-directed mutants revealed that loss of latch interactions or the entire lid enhanced activity against soluble ester substrates, and hydrogen-deuterium exchange (HDX) mass spectrometry revealed that the LCAT lid is extremely dynamic in solution. Upon addition of a covalent inhibitor that mimics one of the reaction intermediates, there is an overall decrease in HDX in the lid and adjacent regions of the protein, consistent with ordering. These data suggest a model wherein the active site of LCAT is shielded from soluble substrates by a dynamic lid until it interacts with HDL to allow transesterification to proceed.
    Mesh-Begriff(e) Apolipoprotein A-I/physiology ; Catalytic Domain ; Crystallography, X-Ray ; Deuterium Exchange Measurement ; Enzyme Activation ; Humans ; Lipoproteins, HDL/metabolism ; Mutagenesis, Site-Directed ; Phosphatidylcholine-Sterol O-Acyltransferase/chemistry ; Phosphatidylcholine-Sterol O-Acyltransferase/metabolism ; Protein Conformation
    Chemische Substanzen APOA1 protein, human ; Apolipoprotein A-I ; Lipoproteins, HDL ; Phosphatidylcholine-Sterol O-Acyltransferase (EC 2.3.1.43)
    Sprache Englisch
    Erscheinungsdatum 2017-10-13
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M117.802736
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel: Structural requirements for antioxidative and anti-inflammatory properties of apolipoprotein A-I mimetic peptides.

    Anantharamaiah, G M / Mishra, Vinod K / Garber, David W / Datta, Geeta / Handattu, Shaila P / Palgunachari, Mayakonda N / Chaddha, Manjula / Navab, Mohamad / Reddy, Srinivasa T / Segrest, Jere P / Fogelman, Alan M

    Journal of lipid research

    2007  Band 48, Heft 9, Seite(n) 1915–1923

    Abstract: ... the structure and function of apoA-I and HDL through studies of the amphipathic helix motif may lead to peptide ... A-I (apoA-I), the major protein component of HDL, the molecular basis for its antiatherogenic and ... anti-inflammatory functions remain elusive. Another protein component of HDL, apoA-II, has structural features ...

    Abstract Recently, attention has been focused on pharmacological treatments that increase HDL cholesterol to prevent coronary artery disease. Despite three decades of extensive research of human apolipoprotein A-I (apoA-I), the major protein component of HDL, the molecular basis for its antiatherogenic and anti-inflammatory functions remain elusive. Another protein component of HDL, apoA-II, has structural features similar to those of apoA-I but does not possess atheroprotective properties. To understand the molecular basis for the effectiveness of apoA-I, we used model synthetic peptides. We designed analogs of the class A amphipathic helical motif in apoA-I that is responsible for solubilizing phospholipids. None of these analogs has sequence homology to apoA-I, but all are similar in their lipid-associating structural motifs. Although all of these peptide analogs interact with phospholipids to form peptide:lipid complexes, the biological properties of these analogs are different. Physical-chemical and NMR studies of these peptides have enabled the delineation of structural requirements for atheroprotective and anti-inflammatory properties in these peptides. It has been shown that peptides that interact strongly with lipid acyl chains do not have antiatherogenic and anti-inflammatory properties. In contrast, peptides that associate close to the lipid head group (and hence do not interact strongly with the lipid acyl chain) are antiatherogenic and anti-inflammatory. Understanding the structure and function of apoA-I and HDL through studies of the amphipathic helix motif may lead to peptide-based therapies for inhibiting atherosclerosis and other related inflammatory lipid disorders.
    Mesh-Begriff(e) Animals ; Anti-Inflammatory Agents/therapeutic use ; Antioxidants/therapeutic use ; Apolipoprotein A-I/chemistry ; Apolipoprotein A-I/therapeutic use ; Apolipoproteins A/therapeutic use ; Atherosclerosis/drug therapy ; Biomimetic Materials/therapeutic use ; Cholesterol, HDL/physiology ; Humans ; Models, Molecular ; Protein Structure, Secondary ; Structure-Activity Relationship
    Chemische Substanzen Anti-Inflammatory Agents ; Antioxidants ; Apolipoprotein A-I ; Apolipoproteins A ; Cholesterol, HDL
    Sprache Englisch
    Erscheinungsdatum 2007-06-14
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 80154-9
    ISSN 1539-7262 ; 0022-2275
    ISSN (online) 1539-7262
    ISSN 0022-2275
    DOI 10.1194/jlr.R700010-JLR200
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel: Structural requirements for antioxidative and anti-inflammatory properties of apolipoprotein A-I mimetic peptides

    Anantharamaiah, G.M / Mishra, Vinod K / Garber, David W / Datta, Geeta / Handattu, Shaila P / Palgunachari, Mayakonda N / Chaddha, Manjula / Navab, Mohamad / Reddy, Srinivasa T / Segrest, Jere P / Fogelman, Alan M

    Journal of lipid research JLR. 2007 Sept., v. 48, no. 9

    2007  

    Abstract: ... the structure and function of apoA-I and HDL through studies of the amphipathic helix motif may lead to peptide ... A-I (apoA-I), the major protein component of HDL, the molecular basis for its antiatherogenic and ... anti-inflammatory functions remain elusive. Another protein component of HDL, apoA-II, has structural features ...

    Abstract Recently, attention has been focused on pharmacological treatments that increase HDL cholesterol to prevent coronary artery disease. Despite three decades of extensive research of human apolipoprotein A-I (apoA-I), the major protein component of HDL, the molecular basis for its antiatherogenic and anti-inflammatory functions remain elusive. Another protein component of HDL, apoA-II, has structural features similar to those of apoA-I but does not possess atheroprotective properties. To understand the molecular basis for the effectiveness of apoA-I, we used model synthetic peptides. We designed analogs of the class A amphipathic helical motif in apoA-I that is responsible for solubilizing phospholipids. None of these analogs has sequence homology to apoA-I, but all are similar in their lipid-associating structural motifs. Although all of these peptide analogs interact with phospholipids to form peptide:lipid complexes, the biological properties of these analogs are different. Physical-chemical and NMR studies of these peptides have enabled the delineation of structural requirements for atheroprotective and anti-inflammatory properties in these peptides. It has been shown that peptides that interact strongly with lipid acyl chains do not have antiatherogenic and anti-inflammatory properties. In contrast, peptides that associate close to the lipid head group (and hence do not interact strongly with the lipid acyl chain) are antiatherogenic and anti-inflammatory. Understanding the structure and function of apoA-I and HDL through studies of the amphipathic helix motif may lead to peptide-based therapies for inhibiting atherosclerosis and other related inflammatory lipid disorders.
    Sprache Englisch
    Erscheinungsverlauf 2007-09
    Umfang p. 1915-1923.
    Erscheinungsort American Society for Biochemistry and Molecular Biology
    Dokumenttyp Artikel
    ZDB-ID 80154-9
    ISSN 1539-7262 ; 0022-2275
    ISSN (online) 1539-7262
    ISSN 0022-2275
    Datenquelle NAL Katalog (AGRICOLA)

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