Biotuotteiden ja biotekniikan laitos

Solujen muokkaus

Apulaisprofessori Sesilja Arangon johtama Solujen muokkaus -tutkimusryhmä kehittää menetelmiä proteiinien biomolekylaariseen konjugaatioon sekä entsymaattisiin post-translationaalisiin muokkauksiin mukaan lukien fosforylaatiot, hydroksylaatiot ja glykosylaatiot. Tutkimustamme motivoivat kehittämiemme menetelmien lukuisat sovellukset proteiinien ja peptidien puhdistuksesta funktionalisointiin. Keskitymme erityisesti biomateriaaleina hyödynnettävien proteiinien, kuten silkkien ja kollageenien, muokkaamiseen. Tavoitteemme on kehittää uudenlaisia ympäristöystävällisiä materiaaleja, joilla on erinomaiset mekaaniset ominaisuudet sekä täysin uudenlaisia toiminnallisuuksia.
kinaasi
Kuvan komposiitti: Sesilja Aranko

Tutkimusteemoja

  • Protein ligases
  • Post-translational modifications in bacteria
  • Microbial production
  • Folding and assembly mechanisms of silk and collagen proteins
Assembly: Sesilja Aranko. Collagen protein and film, fluorescent silk protein, silk fibers
Composite image: Sesilja Aranko

Examples of ongoing research projects

Functional and water-resistant composite materials from crosslinked non-canonical silks and cellulose (CrossSilk)

In this project, funded by the Research Council of Finland (formerly the Academy of Finland), we aim to improve the water resistance of currently available silk- and cellulose-based biomaterials by mimicking the crosslinking of natural silks and leather. The goal is to design fully biodegradable materials with outstanding mechanical properties in both dry and wet states. We hope that the novel crosslinked silk-CNF composite materials developed in the project can be used as a renewable and biodegradable alternative to replace current plastic- and animal-based materials. 

https://research.aalto.fi/en/projects/crosssilk

From post-translationally modified proteins to functional biomaterials (Pro2Fun)

The goal of this project, funded by the Novo Nordisk Foundation Emerging Investigator grant, is to develop methods to produce post-translationally modified structural proteins, including silks and collagens, in bacteria that cannot make the desired modifications naturally. There is accumulating evidence that the post-translational modifications of proteins are essential for the mechanical properties and functionalities of the resulting materials. Yet, the mechanisms behind how these modifications affect the properties of biomaterials are not fully understood, mainly due to technical limitations. Production in bacteria enables obtaining the proteins in an economical, ethical, and sustainable manner. We use the modified proteins to engineer novel functional biomaterials, which have the potential to substitute current oil- and animal-based alternatives.

Ryhmän jäsenet

 Sesilja Aranko

Sesilja Aranko

Assistant Professor
T107 Bioproducts and Biosystems
 Nea Möttönen

Nea Möttönen

Research Assistant

Stefania Aspholm-Tsironi

Master's student

Katarina Knuuttila

Research assistant

Interested in working with us? 

Contact: [email protected]

Julkaisuja

Sustainable Spinning of Artificial Spider Silk Fibers with Excellent Toughness and Inherent Potential for Functionalization

Ruxia Fan, Katarina Knuuttila, Benjamin Schmuck, Gabriele Greco, Anna Rising, Markus B. Linder, A. Sesilja Aranko 2024 Advanced Functional Materials

Triblock Proteins with Weakly Dimerizing Terminal Blocks and an Intrinsically Disordered Region for Rational Design of Condensate Properties

Dmitrii Fedorov, Nelmary Roas-Escalona, Dmitry Tolmachev, Adam L. Harmat, Alberto Scacchi, Maria Sammalkorpi, A. Sesilja Aranko, Markus B. Linder 2024 Small

Phase separation drives the folding of recombinant collagen

Mengjie Shen, Daniil Astapov, Dmitrii Fedorov, Teemu Välisalmi, Markus B. Linder, A. Sesilja Aranko 2024 International Journal of Biological Macromolecules

Biomolecular Click Reactions Using a Minimal pH-Activated Catcher/Tag Pair for Producing Native-Sized Spider-Silk Proteins

Ruxia Fan, Johanna Hakanpää, Karoliina Elfving, Helena Taberman, Markus B. Linder, A. Sesilja Aranko 2023 Angewandte Chemie - International Edition

Upcycling of Keratin Wastes in Sustainable Textile Fiber Applications

Wenwen Fang, Ruxia Fan, A. Sesilja Aranko, Michael Hummel, Herbert Sixta 2023 ACS Sustainable Chemistry and Engineering

Molecular mechanisms mediating stiffening in the mechanically adaptable connective tissues of sea cucumbers

Marie Bonneel, Elise Hennebert, A. Sesilja Aranko, Dong Soo Hwang, Mathilde Lefevre, Valentine Pommier, Ruddy Wattiez, Jérôme Delroisse, Patrick Flammang 2022 Matrix Biology

Liquid-Liquid Phase Separation and Assembly of Silk-like Proteins is Dependent on the Polymer Length

Laura Lemetti, Alberto Scacchi, Yin Yin, Mengjie Shen, Markus B. Linder, Maria Sammalkorpi, A. Sesilja Aranko 2022 Biomacromolecules

Recombinant Spider Silk Protein and Delignified Wood Form a Strong Adhesive System

Laura Lemetti, Jennifer Tersteegen, Juuso Sammaljärvi, A. Sesilja Aranko, Markus B. Linder 2022 ACS Sustainable Chemistry and Engineering

The Convergence of the Hedgehog/Intein Fold in Different Protein Splicing Mechanisms

Hannes M. Beyer, Salla I. Virtanen, A. Sesilja Aranko, Kornelia M. Mikula, George T. Lountos, Alexander Wlodawer, O. H.Samuli Ollila, Hideo Iwaï 2020 International Journal of Molecular Sciences

Sea star-inspired recombinant adhesive proteins self-assemble and adsorb on surfaces in aqueous environments to form cytocompatible coatings

Mathilde Lefevre, Patrick Flammang, A. Sesilja Aranko, Markus B. Linder, Thomas Scheibel, Martin Humenik, Maxime Leclercq, Mathieu Surin, Lionel Tafforeau, Ruddy Wattiez, Philippe Leclère, Elise Hennebert 2020 Acta Biomaterialia

Substrate specificities of inteins investigated by QuickDrop-cassette mutagenesis

Jesper S. Oeemig, Hannes M. Beyer, A. Sesilja Aranko, Justus Mutanen, Hideo Iwaï 2020 FEBS Letters

Molecular crowding facilitates assembly of spidroin-like proteins through phase separation

Laura Lemetti, Sami Pekka Hirvonen, Dmitrii Fedorov, Piotr Batys, Maria Sammalkorpi, Heikki Tenhu, Markus B. Linder, A. Sesilja Aranko 2019 European Polymer Journal

Biomimetic composites with enhanced toughening using silk-inspired triblock proteins and aligned nanocellulose reinforcements

Pezhman Mohammadi, A. Sesilja Aranko, Christopher P. Landowski, Olli Ikkala, Kristaps Jaudzems, Wolfgang Wagermaier, Markus B. Linder 2019 Science Advances

Phase transitions as intermediate steps in the formation of molecularly engineered protein fibers

Pezhman Mohammadi, Aino Sesilja Aranko, Laura Lemetti, Zoran Cenev, Quan Zhou, Salla Virtanen, Christopher P. Landowski, Merja Penttilä, Wolfgang J. Fischer, Wolfgang Wagermaier, Markus Linder 2018 Communications Biology

Salt-inducible Protein Splicing in cis and trans by Inteins from Extremely Halophilic Archaea as a Novel Protein-Engineering Tool

Annika Ciragan, Sesilja Aranko, Igor Tascon, Hideo Iwaï 2016 Journal of Molecular Biology

Nature's recipe for splitting inteins

Aino Sesilja Aranko, Alexander Wlodawer, Hideo Iwaï 2014 PROTEIN ENGINEERING DESIGN AND SELECTION

Structure-based engineering and comparison of novel split inteins for protein ligation

A. Sesilja Aranko, Jesper S. Oeemig, Dongwen Zhou, Tommi Kajander, Alexander Wlodawer, Hideo Iwaï 2014 Molecular BioSystems

Intermolecular domain swapping induces intein-mediated protein alternative splicing

Sesilja Aranko, Jesper S. Oeemig, Tommi Kajander, Hideo Iwaï 2013 NATURE CHEMICAL BIOLOGY

Protein trans-splicing as a protein ligation tool to study protein structure and function

Sesilja Aranko, Gerrit Volkmanna 2011 BioMolecular Concepts

Use of protein trans-splicing to produce active and segmentally 2H, 15N labeled mannuronan C5-epimerase AlgE4

Edith Buchinger, Finn L. Aachmann, Sesilja Aranko, Svein Valla, Gudmund Skjåk-BræK, Hideo Iwaï, Reinhard Wimmer 2010 Protein Science

Segmental isotopic labeling of multi-domain and fusion proteins by protein trans-splicing in vivo and in vitro

Mikko Muona, Sesilja Aranko, Vytas Raulinaitis, Hideo Iwaï 2010 Nature Protocols

In vivo and in vitro protein ligation by naturally occurring and engineered split DnaE inteins

A. Sesilja Aranko, Sara Züger, Edith Buchinger, Hideo Iwaï 2009 PloS one

Segmental isotopic labeling of a central domain in a multidomain protein by protein traws-splicing using only one robust dnae intein

Alena E L Busche, Sesilja Aranko, Mehdi Talebzadeh-Farooji, Frank Bernhard, Volker Dötsch, Hideo Iwaï 2009 Angewandte Chemie

Solution structure of DnaE intein from Nostoc punctiforme

Jesper S. Oeemig, Sesilja Aranko, Janica Djupsjöbacka, Kimmo Heinämäki, Hideo Iwaï 2009 FEBS Letters

Segmental isotopic labelling of a multidomain protein by protein ligation by protein trans-splicing

Mikko Muona, Sesilja Aranko, Hideo Iwai 2008 ChemBioChem: a European journal of chemical biology
Lisää tietoa tutkimuksestamme löytyy Aallon tutkimusportaalista.
Tutkimusportaali

Käyttämämme tutkimusinfrastruktuurit

Opening of the Aalto Bioproduct Centre

Bioeconomy Infrastructure (ulkoinen linkki)

Joint research infrastructure of Aalto University and VTT Bioeconomy infrastructure on Finland’s roadmap for research infrastructures 2021–2024

Aalto yliopisto piisirulla

OtaNano

Otaniemen mikro- ja nanoteknologioiden infrastruktuuri OtaNano on kansallinen tutkimusinfrastruktuuri kilpailukykyisen tutkimuksen harjoittamiseen nanotieteiden ja -teknologian sekä kvanttiteknologioiden alalla.

Color logo for EMBL with a hexagonal abstract image made up of green and red dots

European Molecular Biology Laboratory (ulkoinen linkki)

With 28 member states, EMBL has more than 110 independent research groups and service teams covering the spectrum of molecular biology at six sites in Barcelona, Grenoble, Hamburg, Heidelberg, EMBL-EBI Hinxton, and Rome.

Sesilja Aranko.

Merkittävä Novo Nordisk -rahoitus tutkija Sesilja Arangolle

Aalto-yliopiston tutkija Sesilja Aranko on saanut Novo Nordisk Fonden -säätiön myöntämän Emerging Investigator -rahoituksen post-translationaalisesti muokattujen proteiinipohjaisten materiaalien kehittämiseen. Viisivuotiselle kaudelle myönnetyn rahoituksen suuruus on 10 miljoonaa DKK (noin 1,34M€).

Uutiset
  • Julkaistu:
  • Päivitetty:
Jaa
URL kopioitu