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Destabilization of Basic Fibroblast Growth Factor by Oligodeoxynucleotides

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Chinese Chemical Letters 2006年第3期17卷 415-418页

作者： Qiang WU Ju WANG Ling ZHANG An HONG Jin Song REN Sub division of Biological Inorganic Chemistry Key Laboratory of Rare Earth Chemistry and Physics Changchun Institute of Applied Chemistry Chinese Academy of Sciences Changchun 130022 Bioengineering Institute of Jinan University Guangzhou 510632

The effects of oligodeoxynucleotide （ODN） on the conformation of basic fibroblast growth factor （bFGF） were studied by spectral method. The results showed that ODN destabilized the protein.

关键词： Basic fibroblast growth factor oligodeoxynucleotide (ODN) conformational changes

Biphasic modulation of chemerin peptide-induced calcium flux and ERK phosphorylation by amyloid beta peptide

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中国药理学与毒理学杂志 2017年第10期31卷 1020-1021页

作者： Hao GONG Shuo ZHANG Dan LIAO Richard Dequan YE School of Pharmacy Shanghai Jiao Tong University Institute of Chinese Medical Sciences University of Macao

OBJECTIVE The chemokine-like receptor 1(CMKLR1,Chem R23) is a functional receptor for chemerin,the chemerin-derived nonapeptide(C9),and the amyloid β peptide 1-42(Aβ_(42)).Because these peptides share little sequence homology,studies were conducted to investigate their pharmacological properties and regulation at *** Cells expressing CMKLR1 were incubated with Aβ_(42) before stimulation with a strong agonist,the C9 *** mobilization,c AMP inhibition and MAP kinase activation were *** FRET were determined using CMKLR1 constructs with an ECFP attached to the C-terminus and a Fl As H binding motif embedded in the first intracellular loop(IL1).RESULTS Binding of both Aβ_(42) and the C9 peptide induced CMKLR1 internalization,but only the Aβ_(42)-induced receptor internalization involved clathrin-coated ***,Aβ_(42) but not C9 stimulated β-arrestin 2 translocation to plasma membranes.A robust Ca^(2+)flux was observed following C9 stimulation,whereas Aβ_(42) was ineffective even at micromolar *** its low potency in calcium mobilization assay,Aβ_(42) was able to alter C9-induced Ca^(2+) flux in dose-dependent manner:a potentiation effect at 100 pmol·L^(-1) of Aβ_(42) was followed by a suppression at 10 nmol·L^(-1) and further potentiation at 1 μmol·L^(-1).This unusual and biphasic modulatory effect was also seen in the C9-induced ERK phosphorylation but the dose curve was opposite to that of Ca^(2+) flux and c AMP inhibition,suggesting a reciprocal regulatory *** FRET assay confirmed that Aβ_(42) modulates CMKLR1 rather than its downstream signaling *** These findings suggest Aβ_(42) as an allosteric modulator that can both positively and negatively regulate the activation state of CMKLR1 in a manner that differs from existing allosteric modulatory mechanisms.

关键词： G protein-coupled receptors allosteric modulation fluorescent resonance energy transfer chemokine like receptor 1 chemerin conformational changes

Functionally diverse ligands modulate different activation states of the formyl peptide receptor 2,a G protein-coupled receptor

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中国药理学与毒理学杂志 2017年第10期31卷 981-982页

作者： Shuo ZHANG Hao GONG Richard Dequan YE School of Pharmacy Shanghai Jiao Tong University Institute of Chinese Medical Sciences University of Macao

OBJECTIVE To identify the mechanisms by which the formyl peptide receptor 2(FPR2)mediates both inflammatory and anti-inflammatory signaling in an agonist-dependent *** Cells expressing FPR2 were incubated with weak agonists,Aβ42 and Ac2-26,before stimulation with a strong agonist,*** mobilization,c AMP inhibition and MAP kinase activation were *** FRET were determined using FPR2 constructs with an ECFP attached to the C-terminus and a Fl As H binding motif embedded in the first or third intracellular loop(IL1 or IL3,respectively).RESULTS Aβ42 did not induce significant Ca^(2+) mobilization,but positively modulated WKYMVm-induced Ca^(2+) mobilization and c AMP reduction in a dose-variable manner within a narrow range of ligand *** FPR2-expressing cells with Ac2-26,a peptide with anti-inflammatory activity,negatively modulated WKYMVm-induced Ca^(2+) mobilization and c AMP *** FRET assay showed that stimulation of the receptor constructs with Aβ42 brought the C-terminal domain closer to IL1 but away from *** opposite conformational change was induced by *** FPR2 conformation induced by Aβ42 corresponded to enhanced ERK phosphorylation and attenuated p38 MAPK phosphorylation,whereas Ac2-26 induced FPR2 conformational change corresponding to elevated p38 MAPK phosphorylation and reduced ERK *** Aβ42 and Ac2-26 induce different conformational changes in *** findings provide a structural basis for FPR2 mediation of inflammatory vs anti-inflammatory functions and identify a type of receptor modulation that differs from the classic positive and negative allosteric modulation.

关键词： G protein-coupled receptors allosteric modulation fluorescent resonance energy transfer formyl peptide receptor 2 conformational changes

The conformational states of talin autoinhibition complex and its activation under forces

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Science China(Life Sciences) 2015年第6期58卷 694-703页

作者： ZENG Yan ZHANG Yong SONG XianQiang JI QingHua YE Sheng ZHANG RongGuang LOU JiZhong Key Laboratory of RNA Biology Institute of Biophysics Chinese Academy of Sciences University of Chinese Academy of Sciences National Laboratory of Biomacromolecules Institute of Biophysics Chinese Academy of Sciences

Talin is an integrin-binding protein located at focal adhesion site and serves as both an adapter and a force transmitter. Its integrin binding activity is regulated by the intramolecular autoinhibition interaction between its F3 and RS domains. Here, we used atomic force microscopy to measure the strength of talin autoinhibition complex. Our results suggest that the lifetime of talin autoinhibition complex shows weak catch bond behavior and does not change significantly at smaller forces, while it drops rapidly at larger forces(>10 p N). Moreover, besides the complex conformation revealed by crystal structure, our molecular dynamics(MD) simulations indicate the possible existence of another stable conformation. Further analysis indicates that forces may regulate the equilibrium of the two stable binding states and result in the non-exponential force dependence of the binding lifetime. Our findings reveal a negative regulation mechanism on talin activation and provide a new point of view on the function of talin in focal adhesion.

关键词： cell adhesion integrin signaling single molecule biophysics molecular dynamics simulations conformational changes

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Investigation of the binding behavior of human serum albumin and phosphorothioate oligodeoxynucleotide

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Journal of Chinese Pharmaceutical Sciences 2007年第1期16卷 9-13页

作者：叶国柱张亮仁张礼和北京大学药学院天然药物及仿生药物国家重点实验室北京100083

Aim To study the binding behavior between human serum albumin （HSA） and phosphorothioate oligodeoxynucleotide （PS- ODN） and the effects of bivalent cations on the interaction. Methods Surface plasma resonance, circular dichroism and fluorescence experiments were conducted. Results （ 1 ） the binding ability was decreased along with the increase of pH; （2） Zn^2＋and Ni^2＋ enhanced the interaction between PS-ODN and HSA; （3） Upon PS-ODN binding, the conformation of HSA was changed with an increase of β - sheet. Conclusion The results provide experimental evidences to the hypothesis that PS-ODN binds with HSA in the positive potential region, and histidine residues located in the region play a crucial rule in the interaction.

关键词： Phosphoruthioate oligodeoxynucleotide Human serum albumin Positive potential region conformational changes