Fibie a 28 ans

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Fibie a 28 ans

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1 Laboratory of Cell Morphology, Institute of Cytology Russian Academy of Science, St. Petersburg, Russia.

2 Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology Russian Academy of Science, St. Petersburg, Russia.

3 Institute of Physics, Nanotechnology and Telecommunications, Peter the Great St. Petersburg Polytechnic University, St. Petersburg, Russia.







M I Sulatsky et al.






Prion .



2020 Dec .







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1 Laboratory of Cell Morphology, Institute of Cytology Russian Academy of Science, St. Petersburg, Russia.

2 Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology Russian Academy of Science, St. Petersburg, Russia.

3 Institute of Physics, Nanotechnology and Telecommunications, Peter the Great St. Petersburg Polytechnic University, St. Petersburg, Russia.



Morphology and staining by fluorescent probes of amyloid fibrils formed from lysozyme (top panels) and insulin (bottom panels) using of buffer solution with pH 6.3. Left panels show transmission electron microscopy (TEM) images of amyloid fibrils in the absence (AF) and in the presence of fluorescent probes ANS (AF+ANS) and ThT (AF+ThT). Data of confocal laser scanning microscopy (CLSM, Right panels) show amyloids stained by these fluorescent probes. The scale bars on the TEM and CLSM images are equal to 1 and 4 µm, respectively.
Photophysical properties of amyloid fibrils formed from lysozyme and insulin using of buffer solution with pH 6.3 and their binding to fluorescent probes ThT and ANS. (a) -Rayleigh Light Scattering (RLS) and (b) – turbidity (at λ = 530 nm) of amyloids. (c) – normalized absorbance and (d) – fluorescence spectra of ANS in free (ANS) and bound to lysozyme (Lys+ANS) and insulin (Ins+ANS) amyloid fibrils states. (e) – normalized absorbance and (f) – fluorescence spectra of ThT in free (ThT) and bound to lysozyme (Lys+ThT) and insulin (Ins+ThT) amyloid fibrils states. CD spectra of (g) lysozyme and (h) insulin amyloid fibrils in the absence (Lys, Ins) and in the presence of fluorescent probes ANS (Lys+ANS, Ins+ANS) and ThT (Lys+ThT, Ins+ThT).
Morphology and photophysical properties of ultrasonicated amyloid fibrils formed from lysozyme and insulin using of buffer solution with pH 6.3 and and their binding to fluorescent probes ThT and ANS. (a), (b) – transmission electron microscopy (TEM) images of amyloid fibrils formed from lysozyme and insulin, respectively, before and after ultrasonication. The scale bars on the images are equal to 500 nm. (c) – normalized absorbance spectra of ANS in free (ANS) and bound to lysozyme (Lys+ANS) and insulin (Ins+ANS) amyloid fibrils states. (d) – normalized absorbance spectra of ThT in free (ThT) and bound to lysozyme (Lys+ThT) and insulin (Ins+ThT) amyloid fibrils states. (e) – Rayleigh Light Scattering (RLS) and (f) turbidity (at λ = 530 nm) of amyloids. CD spectra of (g) lysozyme and (h) insulin amyloid fibrils in the absence (Lys, Ins) and in the presence of fluorescent probes ANS (Lys+ANS, Ins+ANS) and ThT (Lys+ThT, Ins+ThT).
Morphology and staining by fluorescent probes of amyloid fibrils formed from lysozyme (top panels) and insulin (bottom panels) using of buffer solution with pH 2. Left panels show transmission electron microscopy (TEM) images of amyloid fibrils in the absence (AF) and in the presence of fluorescent probes ANS (AF+ANS) and ThT (AF+ThT). Data of confocal laser scanning microscopy images (CLSM, Right panels) show amyloids stained by these fluorescent probes. The scale bars on the TEM and CLSM images are equal to 1 and 4 µm, respectively.
Photophysical properties of amyloid fibrils formed from lysozyme and insulin using of buffer solution with pH 2 and their binding to fluorescent probes ThT and ANS. (a) – Rayleigh Light Scattering (RLS) and (b) – turbidity (at λ = 530 nm) of amyloids. (c) – normalized absorbance and (d) – fluorescence spectra of ANS in free (ANS) and bound to lysozyme (Lys+ANS) and insulin (Ins+ANS) amyloid fibrils states. (e) – normalized absorbance and (f) fluorescence spectra of ThT in free (ThT) and bound to lysozyme (Lys+ThT) and insulin (Ins+ThT) amyloid fibrils states. CD spectra of (g) lysozyme and (h) insulin amyloid fibrils in the absence (Lys, Ins) and in the presence of fluorescent probes ANS (Lys+ANS, Ins+ANS) and ThT (Lys+ThT, Ins+ThT).


Stepanenko OV, Sulatsky MI, Mikhailova EV, Stepanenko OV, Kuznetsova IM, Turoverov KK, Sulatskaya AI.
Stepanenko OV, et al.
Int J Mol Sci. 2021 May 2;22(9):4828. doi: 10.3390/ijms22094828.
Int J Mol Sci. 2021.

PMID: 34063223
Free PMC article.







Ziaunys M, Smirnovas V.
Ziaunys M, et al.
J Phys Chem B. 2019 Oct 17;123(41):8727-8732. doi: 10.1021/acs.jpcb.9b08652. Epub 2019 Oct 8.
J Phys Chem B. 2019.

PMID: 31580671








Sulatskaya AI, Rodina NP, Polyakov DS, Sulatsky MI, Artamonova TO, Khodorkovskii MA, Shavlovsky MM, Kuznetsova IM, Turoverov KK.
Sulatskaya AI, et al.
Int J Mol Sci. 2018 Sep 14;19(9):2762. doi: 10.3390/ijms19092762.
Int J Mol Sci. 2018.

PMID: 30223436
Free PMC article.







Biancalana M, Koide S.
Biancalana M, et al.
Biochim Biophys Acta. 2010 Jul;1804(7):1405-12. doi: 10.1016/j.bbapap.2010.04.001. Epub 2010 Apr 22.
Biochim Biophys Acta. 2010.

PMID: 20399286
Free PMC article.

Review.





Verma S, Ravichandiran V, Ranjan N.
Verma S, et al.
Biochimie. 2021 Nov;190:111-123. doi: 10.1016/j.biochi.2021.06.003. Epub 2021 Jun 9.
Biochimie. 2021.

PMID: 34118329


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Onchaiya S, Saotome T, Mizutani K, Martinez JC, Tame JRH, Kidokoro SI, Kuroda Y.
Onchaiya S, et al.
Molecules. 2022 Apr 28;27(9):2813. doi: 10.3390/molecules27092813.
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PMID: 35566161
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Vignon A, Salvador-Prince L, Lehmann S, Perrier V, Torrent J.
Vignon A, et al.
Int J Mol Sci. 2021 Aug 16;22(16):8769. doi: 10.3390/ijms22168769.
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Zuo R, Liu R, Olguin J, Hudalla GA.
Zuo R, et al.
J Phys Chem B. 2021 Jun 24;125(24):6559-6571. doi: 10.1021/acs.jpcb.1c02083. Epub 2021 Jun 15.
J Phys Chem B. 2021.

PMID: 34128680
Free PMC article.







Stepanenko OV, Sulatsky MI, Mikhailova EV, Stepanenko OV, Kuznetsova IM, Turoverov KK, Sulatskaya AI.
Stepanenko OV, et al.
Int J Mol Sci. 2021 May 2;22(9):4828. doi: 10.3390/ijms22094828.
Int J Mol Sci. 2021.

PMID: 34063223
Free PMC article.







Obstarczyk P, Lipok M, Grelich-Mucha M, Samoć M, Olesiak-Bańska J.
Obstarczyk P, et al.
J Phys Chem Lett. 2021 Feb 11;12(5):1432-1437. doi: 10.1021/acs.jpclett.0c03511. Epub 2021 Feb 1.
J Phys Chem Lett. 2021.

PMID: 33522819
Free PMC article.





This work was supported by grant from Russian Science Foundation № 18-74-10100 (experiments with lysozyme amyloids), RF President Fellowships SP-841.2018.4 (experiments with insulin amyloids) and SP-259.2019.4 (analysis of ANS binding to monomeric proteins).

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Fluorescent probes thioflavin T (ThT) and 1-anilino-8-naphthalene sulfonate (ANS) are widely used to study amyloid fibrils that accumulate in the body of patients with serious diseases, such as Alzheimer's, Parkinson's, prion diseases, etc. However, the possible effect of these probes on amyloid fibrils is not well understood. In this work, we investigated the photophysical characteristics, structure, and morphology of mature amyloid fibrils formed from two model proteins, insulin and lysozyme, in the presence of ThT and ANS. It turned out that ANS affects the secondary structure of amyloids (shown for fibrils formed from insulin and lysozyme) and their fibers clusterization (valid for lysozyme fibrils), while ThT has no such effects. These results confirm the differences in the mechanisms of these dyes interaction with amyloid fibrils. Observed effect of ANS was explained by the electrostatic interactions between the dye molecule and cationic groups of amyloid-forming proteins (unlike hydrophobic binding of ThT) that induce amyloids conformational changes. This interaction leads to weakening repulsion between positive charges of amyloid fibrils and can promote their clusterization. It was shown that when fibrillogenesis conditions and, consequently, fibrils structure is changing, as well as during defragmentation of amyloids by ultrasonication, the influence of ANS to amyloids does not change, which indicates the universality of the detected effects. Based on the obtained results, it was concluded that ANS should be used cautiously for the study of amyloid fibrils, since this fluorescence probe have a direct effect on the object of study.




Keywords:


1-anilino-8-naphthalene sulfonate (ANS); Amyloid fibrils; fluorescent probes; morphology; secondary structure; thioflavin T (ThT); ultrasonication.

Morphology and staining by fluorescent…
Morphology and staining by fluorescent probes of amyloid fibrils formed from lysozyme (top…
Photophysical properties of amyloid fibrils…
Photophysical properties of amyloid fibrils formed from lysozyme and insulin using of buffer…
Morphology and photophysical properties of…
Morphology and photophysical properties of ultrasonicated amyloid fibrils formed from lysozyme and insulin…
Morphology and staining by fluorescent…
Morphology and staining by fluorescent probes of amyloid fibrils formed from lysozyme (top…
Photophysical properties of amyloid fibrils…
Photophysical properties of amyloid fibrils formed from lysozyme and insulin using of buffer…

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Famille nomade à vélo



Depuis 2010 nous sommes nomades sur les routes du monde.
De la Chine à l'Alaska, de la Syrie à la Nouvelle-Zélande. Nos deux filles sont nées en chemin. Nayla a appris à marcher face aux temples d'Angkor. Fibie a fait ses premiers dans une yourte en Mongolie.



Consulter le profil


Nous avons été appelés en Suisse, nous le
sentons. Présenter la Suisse à Fibie, ainsi
que sa famille, serrer ceux que l’on aime
contre nos cœurs, faisaient partie de ce
passage. Nous avons aussi ressenti que
nous étions là pour transmettre. C’est ainsi
que nous avons donnés des ateliers et plus
de 35 conférences en à peine trois mois.
Ces conférences étaient une invitation à
plonger dans l’inconnu.

Nous y avons parlé de la peur. De la peur du premier
pas vers la vie qui vibre pour nous et surtout des
peurs intérieures que nous portons en chacun de nous.
Si les participants sont arrivés avec des questions
plein la tête, ils sont repartis avec des questions plein
le cœur, selon les témoignages que nous avons reçus.
Nous sentons alors que nous ouvrons une nouvelle
porte. Nos expériences en tant que nomades en
famille ne sont pas uniquement une initiation
personnelle, en les partageant, elles deviennent des
initiations pour d’autres. Nayla et Fibie participeront
aussi à parler en public, chanter en chinois ou dire
quelques mots en japonais. Nayla prendra la parole
pour répondre aux questions, dans une aisance
remarquable.
Nous partageons alors nos dernières
conférences à Grindelwald et à Zermatt. Nous
terminons ainsi ces quelques mois face à l’Eiger et au
Cervin dans les prairies alpines recouvertes de fleurs
sauvages. Fibie, qui n’a pas encore 5 ans, marche
dans les petits sentiers pédestres, dévalant les pentes
ou courant vers les sommets pendant 6 heures. Les
paysages suisses sont éblouissants, une pureté s’y
dévoile. Toutes ces explorations nous ont permis de
nous relier à l’énergie de la Terre suisse, de sa source
d’inspiration et d’élévation. 
____________ ____________ ____________ _______

From Wikipedia, the free encyclopedia
This is the latest accepted revision , reviewed on 18 August 2022 .

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