Spectroscopic and Lipid Binding Studies on the Amino and Carboxyl Terminal Fragments of Locusta migratoria Apolipophorin III

Biochemistry ◽  
1995 ◽  
Vol 34 (37) ◽  
pp. 11822-11830 ◽  
Author(s):  
Vasanthy Narayanaswami ◽  
Paul M. M. Weers ◽  
Jan Bogerd ◽  
Frank P. Kooiman ◽  
Cyril M. Kay ◽  
...  
Keyword(s):  
Locusta Migratoria ◽  
Lipid Binding ◽  
Binding Studies ◽  
Apolipophorin Iii ◽  
Carboxyl Terminal

scholarly journals Initiation of lipid binding in Locusta migratoria apolipophorin III

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Yin Mei Phung ◽  
Johana Rodriguez ◽  
Daisy Martinon ◽  
Gezman Abdullahi ◽  
Paul M. M. Weers
Keyword(s):  
Locusta Migratoria ◽  
Lipid Binding ◽  
Apolipophorin Iii

scholarly journals Fragments of Locusta migratoria apoLp-III provide insight into lipid binding

BBA Advances ◽  
2021 ◽  
pp. 100020
Author(s):  
Blair A. Russell ◽  
James V.C. Horn ◽  
Paul M.M. Weers
Keyword(s):  
Locusta Migratoria ◽  
Lipid Binding ◽  
Insight Into

scholarly journals Structural characterization and in vitro lipid binding studies of non-specific lipid transfer protein 1 (nsLTP1) from fennel (Foeniculum vulgare) seeds

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Mekdes Megeressa ◽  
Bushra Siraj ◽  
Shamshad Zarina ◽  
Aftab Ahmed
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
3D Structure ◽  
Lipid Binding ◽  
Lipid Transfer ◽  
Binding Studies ◽  
Foeniculum Vulgare ◽  
Complete Amino Acid Sequence ◽  
Specific Lipid

AbstractNon-specific lipid transfer proteins (nsLTPs) are cationic proteins involved in intracellular lipid shuttling in growth and reproduction, as well as in defense against pathogenic microbes. Even though the primary and spatial structures of some nsLTPs from different plants indicate their similar features, they exhibit distinct lipid-binding specificities signifying their various biological roles that dictate further structural study. The present study determined the complete amino acid sequence, in silico 3D structure modeling, and the antiproliferative activity of nsLTP1 from fennel (Foeniculum vulgare) seeds. Fennel is a member of the family Umbelliferae (Apiaceae) native to southern Europe and the Mediterranean region. It is used as a spice medicine and fresh vegetable. Fennel nsLTP1 was purified using the combination of gel filtration and reverse-phase high-performance liquid chromatography (RP-HPLC). Its homogeneity was determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry. The purified nsLTP1 was treated with 4-vinyl pyridine, and the modified protein was then digested with trypsin. The complete amino acid sequence of nsLTP1 established by intact protein sequence up to 28 residues, overlapping tryptic peptides, and cyanogen bromide (CNBr) peptides. Hence, it is confirmed that fennel nsLTP1 is a 9433 Da single polypeptide chain consisting of 91 amino acids with eight conserved cysteines. Moreover, the 3D structure is predicted to have four α-helices interlinked by three loops and a long C-terminal tail. The lipid-binding property of fennel nsLTP1 is examined in vitro using fluorescent 2-p-toluidinonaphthalene-6-sulfonate (TNS) and validated using a molecular docking study with AutoDock Vina. Both of the binding studies confirmed the order of binding efficiency among the four studied fatty acids linoleic acid > linolenic acid > Stearic acid > Palmitic acid. A preliminary screening of fennel nsLTP1 suppressed the growth of MCF-7 human breast cancer cells in a dose-dependent manner with an IC50 value of 6.98 µM after 48 h treatment.

scholarly journals Role of the N- and C-Terminal Helices in Apolipophorin III Stability and Lipid Binding

2012 ◽  
Vol 102 (3) ◽  
pp. 58a
Author(s):  
Pankaj Dwivedi ◽  
Johana Rodriguez ◽  
Paul M.M. Weers
Keyword(s):  
Lipid Binding ◽  
Apolipophorin Iii

Structure of the Asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-aminoethylphosphonate as a constituent of a glycoprotein

Biochemistry ◽  
1993 ◽  
Vol 32 (3) ◽  
pp. 766-775 ◽  
Author(s):  
Karl Hard ◽  
Jan M. VAn Doorn ◽  
Jane E. Thomas-Oates ◽  
Johannis P. Kamerling ◽  
Dick J. Van der Horst
Keyword(s):  
Locusta Migratoria ◽  
Apolipophorin Iii

Role of charged amino acid side chains in the stability and lipid binding ofManduca sexta apolipophorin III

1995 ◽  
Vol 30 (2-3) ◽  
pp. 211-223 ◽  
Author(s):  
Minal Upadhyaya ◽  
Kim Oikawa ◽  
Cyril M. Kay ◽  
Douglas G. Scraba ◽  
Roger Bradley ◽  
...  
Keyword(s):  
Amino Acid ◽  
Lipid Binding ◽  
Side Chains ◽  
Apolipophorin Iii ◽  
Amino Acid Side Chains ◽  
The Stability

Structural and Binding Characteristics of the Carboxyl Terminal Fragment of Apolipophorin III from Manduca sexta

Biochemistry ◽  
1994 ◽  
Vol 33 (45) ◽  
pp. 13312-13320 ◽  
Author(s):  
Vasanthy Narayanaswami ◽  
Cyril M. Kay ◽  
Kim Oikawa ◽  
Robert O. Ryan
Keyword(s):  
Manduca Sexta ◽  
Binding Characteristics ◽  
Apolipophorin Iii ◽  
Terminal Fragment ◽  
Carboxyl Terminal

scholarly journals Structural Basis for the Recognition and Cross-linking of Amyloid Fibrils by Human Apolipoprotein E

2007 ◽  
Vol 282 (49) ◽  
pp. 35831-35841 ◽  
Author(s):  
Menachem J. Gunzburg ◽  
Matthew A. Perugini ◽  
Geoffrey J. Howlett
Keyword(s):  
Amyloid Fibrils ◽  
Lipid Binding ◽  
Structural Basis ◽  
Distribution Analysis ◽  
Cross Link ◽  
Binding Studies ◽  
Diverse Range ◽  
Apo E ◽  
Aβ Fibrils ◽  
Terminal Domains

Apolipoprotein (apo) E is a well characterized lipid-binding protein in plasma that also exists as a common nonfibrillar component of both cerebral and systemic amyloid deposits. A genetic link between a common isoform of apoE, apoE4, and the incidence of late onset Alzheimer disease has drawn considerable attention to the potential roles of apoE in amyloid-related disease. We examined the interactions of apoE with amyloid fibrils composed of apoC-II and the amyloid-β (Aβ) peptide. Aggregates of apoE with Aβ and apoC-II are found in Alzheimer and atherosclerotic plaques, respectively. Sedimentation velocity and fibril size distribution analysis showed that apoE3 and E4 isoforms bind and noncovalently cross-link apoC-II fibrils in a similar manner. This ability to cross-link apoC-II fibrils was abolished by the dissociation of the apoE tetramer to monomers or by thrombin cleavage to yield separate N- and C-terminal domains. Preparative ultracentrifuge binding studies indicated that apoE and the isolated N- and C-terminal domains of apoE bind with submicromolar affinities to both apoC-II and Aβ fibrils. Fluorescence quenching and resonance energy transfer experiments confirmed that both domains of apoE interact with apoC-II fibrils and demonstrated that the binding of the isolated N-terminal domain of apoE to apoC-II or Aβ fibrils is accompanied by a significant conformational change with helix three of the domain moving relative to helix one. We propose a model involving the interaction of apoE with patterns of aligned residues that could explain the general ability of apoE to bind to a diverse range of amyloid fibrils.

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