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Rydberg, Johan
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Publikasjoner (10 av 11) Visa alla publikasjoner
Rydberg, J., Baltzer, L. & Sarojini, V. (2013). Intrinsically unstructured proteins by designelectrostatic interactions can control binding, folding, and function of a helix-loop-helix heterodimer. Journal of Peptide Science, 19(8), 461-469
Åpne denne publikasjonen i ny fane eller vindu >>Intrinsically unstructured proteins by designelectrostatic interactions can control binding, folding, and function of a helix-loop-helix heterodimer
2013 (engelsk)Inngår i: Journal of Peptide Science, ISSN 1075-2617, E-ISSN 1099-1387, Vol. 19, nr 8, s. 461-469Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Intrinsically disordered proteins that exist as unordered monomeric structures in aqueous solution at pH7 but fold into four-helix bundles upon binding to recognized polypeptide targets have been designed. NMR and CD spectra of the monomeric polypeptides show the hallmarks of unordered structures, whereas in the bound state they are highly helical. Analytical ultracentrifugation data shows that the polypeptides bind to their targets to form exclusively heterodimers at neutral pH. To demonstrate the relationship between binding, folding, and function, a catalytic site for ester hydrolysis was introduced into an unordered and largely inactive monomer, but that was structured and catalytically active in the presence of a specific polypeptide target. Electrostatic interactions between surface-exposed residues inhibited the binding and folding of the monomers at pH7. Charge-charge repulsion between ionizable amino acids was thus found to be sufficient to disrupt binding between polypeptide chains despite their inherent propensities for structure formation and may be involved in the folding and function of inherently disordered proteins in biology.

sted, utgiver, år, opplag, sider
Wiley-Blackwell, 2013
Emneord
heterodimer, electrostatic interactions, folding, catalysis
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-95940 (URN)10.1002/psc.2520 (DOI)000321703200001 ()
Merknad

Funding Agencies|Swedish Research Council||Swedish Foundation for Strategic Research||

Tilgjengelig fra: 2013-08-19 Laget: 2013-08-12 Sist oppdatert: 2017-12-06
Aili, D., Enander, K., Rydberg, J., Nesterenko, I., Björefors, F., Baltzer, L. & Liedberg, B. (2008). Controlled Assembly of Gold Nanoparticles using De Novo Designed Polypeptide Scaffolds. In: Proceedings SPIE, Vol. 6885, Photonic Biosensing and Microoptics: (pp. 688506-1-688506-8).
Åpne denne publikasjonen i ny fane eller vindu >>Controlled Assembly of Gold Nanoparticles using De Novo Designed Polypeptide Scaffolds
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2008 (engelsk)Inngår i: Proceedings SPIE, Vol. 6885, Photonic Biosensing and Microoptics, 2008, s. 688506-1-688506-8Konferansepaper, Publicerat paper (Fagfellevurdert)
Abstract [en]

Heterodimerization between designed helix-loop-helix polypeptides was utilized in order to assemble gold nanoparticles on planar substrates. The peptides were designed to fold into four-helix bundles upon dimerization. A Cys-residue in the loop region was used to immobilize one of the complementary peptides on a maleimide containing SAM on planar gold substrates whereas the second peptide was immobilized directly on gold nanoparticles. Introducing the peptide decorated particles over a peptide functionalized surface resulted in particle assembly. Further, citrate stabilized particles were assembled on amino-silane modified glass and silicon substrates. By subsequently introducing peptides and gold nanoparticles, particle-peptide hybrid multi layers could be formed.

Emneord
Heterodimerization, polypeptides, gold nanoparticles, four-helix bundle, helix-loop-helix, self-assembly
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-15118 (URN)10.1117/12.775806 (DOI)
Tilgjengelig fra: 2008-10-16 Laget: 2008-10-16 Sist oppdatert: 2018-01-12bibliografisk kontrollert
Aili, D., Enander, K., Rydberg, J., Nesterenko, I., Björefors, F., Baltzer, L. & Liedberg, B. (2008). Folding Induced Assembly of Polypeptide Decorated Gold Nanoparticles. Journal of the American Chemical Society, 130(17), 5780-5788
Åpne denne publikasjonen i ny fane eller vindu >>Folding Induced Assembly of Polypeptide Decorated Gold Nanoparticles
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2008 (engelsk)Inngår i: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 130, nr 17, s. 5780-5788Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Reversible assembly of gold nanoparticles controlled by the homodimerization and folding of an immobilized de novo designed synthetic polypeptide is described. In solution at neutral pH, the polypeptide folds into a helix–loop–helix four-helix bundle in the presence of zinc ions. When immobilized on gold nanoparticles, the addition of zinc ions induces dimerization and folding between peptide monomers located on separate particles, resulting in rapid particle aggregation. The particles can be completely redispersed by removal of the zinc ions from the peptide upon addition of EDTA. Calcium ions, which do not induce folding in solution, have no effect on the stability of the peptide decorated particles. The contribution from folding on particle assembly was further determined utilizing a reference peptide with the same primary sequence but containing both D and L amino acids. Particles functionalized with the reference peptide do not aggregate, as the peptides are unable to fold. The two peptides, linked to the nanoparticle surface via a cysteine residue located in the loop region, form submonolayers on planar gold with comparable properties regarding surface density, orientation, and ability to interact with zinc ions. These results demonstrate that nanoparticle assembly can be induced, controlled, and to some extent tuned, by exploiting specific molecular interactions involved in polypeptide folding.

sted, utgiver, år, opplag, sider
ACS Publications, 2008
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-15116 (URN)10.1021/ja711330f (DOI)
Tilgjengelig fra: 2008-10-16 Laget: 2008-10-16 Sist oppdatert: 2018-01-12bibliografisk kontrollert
Aili, D., Enander, K., Rydberg, J., Lundström, I., Baltzer, L. & Liedberg, B. (2006). Aggregation-Induced Folding of a de novo Designed Polypeptide Immobilized on Gold Nanoparticles. Journal of the American Chemical Society, 128(7), 2194 -2195
Åpne denne publikasjonen i ny fane eller vindu >>Aggregation-Induced Folding of a de novo Designed Polypeptide Immobilized on Gold Nanoparticles
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2006 (engelsk)Inngår i: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 128, nr 7, s. 2194 -2195Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

This communication reports the first steps in the construction of a novel, nanoparticle-based hybrid material for biomimetic and biosensor applications. Gold nanoparticles were modified with synthetic polypeptides to enable control of the particle aggregation state in a switchable manner, and particle aggregation was, in turn, found to induce folding of the immobilized peptides.

sted, utgiver, år, opplag, sider
ACS Publications, 2006
Emneord
Not aviable
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-14041 (URN)10.1021/ja057056j (DOI)
Tilgjengelig fra: 2006-09-28 Laget: 2006-09-28 Sist oppdatert: 2018-01-13bibliografisk kontrollert
Rydberg, J., Vijayalekshmi, S. & Baltzer, L. (2006). Intrinsically unstructured proteins by design: electrostatic interactions can control binding, folding and function of a helix-loop-helix heterodimer.
Åpne denne publikasjonen i ny fane eller vindu >>Intrinsically unstructured proteins by design: electrostatic interactions can control binding, folding and function of a helix-loop-helix heterodimer
2006 (engelsk)Artikkel i tidsskrift (Fagfellevurdert) Submitted
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-14038 (URN)
Tilgjengelig fra: 2006-09-28 Laget: 2006-09-28
Rydberg, J. (2006). Protein-protein interactions in model systems: design, control of catalytic activity and biosensor applications. (Doctoral dissertation). Linköping: Linköping University Electronic Press
Åpne denne publikasjonen i ny fane eller vindu >>Protein-protein interactions in model systems: design, control of catalytic activity and biosensor applications
2006 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

This thesis describes the design of polypeptides, unordered in the monomeric state but capable of folding into helix-loop-helix motifs and dimerise to form four-helix bundles. The goal of the design was to encode them with the capacity to form dimers highly selectively and the ability to carry out molecular functions in the folded state but not in the unordered state, and thus to establish a molecular link between recognition and function. The 42-residue sequences JR2E and JR2K were both shown by CD spectroscopy to adopt unordered conformations under single solute conditions at pH 7 but to form helical conformations in a 1:1 mixture. Analytical ultracentrifugation showed that JR2E and JR2K formed a clean heterodimer and the dissociation constant Kd, measured by CD spectroscopy, was found to be 5 ± 1 μM. Discrimination was enabled by the incorporation of charged residues at the dimer interface in the helical segments of the helix-loop-helix motif. Glutamic acids were incorporated in JR2E and lysines in JR2K, and charge repulsion prevented the monomeric subunits from forming homodimers. In mixtures, however, highly helical heterodimers were formed. The cooperative transition from unordered conformation to heterodimeric four-helix bundle was exploited in the design of a signal response system by incorporating a reactive site, capable of catalysing the hydrolysis of a m-nitrophenyl ester, into the negatively charged polypeptide. In the unfolded state the functionalised polypeptide was virtually inactive but in the folded state, induced by the interaction with JR2K, the substrate was hydrolysed approximately an order of magnitude more efficiently.

Interactions between the designed polypeptides and a functionalised polythiophene polymer were studied and it was found that the conformation of the polymer was controlled by the polypeptides, largely by electrostatic interactions. The negatively charged JR2E forced the polymer to adopt a planar conformation while the positively charged JR2K induced a more twisted conformation of the polymer. The spectral changes coupled to the conformational transitions of the polymer were used to measure the binding of human Carbonic anhydrase II by JR2E functionalised with a benzenesulphonamide ligand, in demonstration of its use as a tool for high-throughput screening.

JR2E immobilised on gold nanoparticles was shown to form homodimers reversibly under pH control, with affinities large enough to determine the state of aggregation of the gold nanoparticles.

sted, utgiver, år, opplag, sider
Linköping: Linköping University Electronic Press, 2006
Serie
Linköping Studies in Science and Technology. Dissertations, ISSN 0345-7524 ; 1037
Emneord
Chemistry, Protein interactions, design, catalysis, biosensors, hybride materials, nanoparticles, Kemi
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-7485 (URN)91-85523-19-4 (ISBN)
Disputas
2006-09-22, Planck, Fysikhuset, Campus Valla, Linköpings universitet, Linköping, 09:15 (engelsk)
Opponent
Veileder
Tilgjengelig fra: 2006-09-28 Laget: 2006-09-28 Sist oppdatert: 2009-04-01bibliografisk kontrollert
Aili, D., Enander, K., Rydberg, J., Lundström, I., Baltzer, L. & Liedberg, B. (2004). Alpha helix-inducing dimerization of synthetic polypeptide scaffolds on gold - a model system for receptor mimicking and biosensing. In: 8th World Congress on Biosensors,2004.
Åpne denne publikasjonen i ny fane eller vindu >>Alpha helix-inducing dimerization of synthetic polypeptide scaffolds on gold - a model system for receptor mimicking and biosensing
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2004 (engelsk)Inngår i: 8th World Congress on Biosensors,2004, 2004Konferansepaper, Publicerat paper (Annet vitenskapelig)
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-42427 (URN)64001 (Lokal ID)64001 (Arkivnummer)64001 (OAI)
Tilgjengelig fra: 2009-10-10 Laget: 2009-10-10 Sist oppdatert: 2014-10-08
Aili, D., Enander, K., Rydberg, J., Lundström, I., Baltzer, L. & Liedberg, B. (2004). Folding-induced aggregation of polypeptide-decorated gold nanoparticles - an nano-scale Lego for the construction of complex hybrid materials. In: 5th International Conference on Biological Physics,2004.
Åpne denne publikasjonen i ny fane eller vindu >>Folding-induced aggregation of polypeptide-decorated gold nanoparticles - an nano-scale Lego for the construction of complex hybrid materials
Vise andre…
2004 (engelsk)Inngår i: 5th International Conference on Biological Physics,2004, 2004Konferansepaper, Publicerat paper (Annet vitenskapelig)
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-42426 (URN)64000 (Lokal ID)64000 (Arkivnummer)64000 (OAI)
Tilgjengelig fra: 2009-10-10 Laget: 2009-10-10 Sist oppdatert: 2014-10-08
Nilsson, P., Rydberg, J., Baltzer, L. & Inganäs, O. (2004). Twisting macromolecular chains: self-assembly of a chiral supermolecule from nonchiral polythiophene polyanions and random-coil synthetic peptides. Proceedings of the National Academy of Sciences of the United States of America, 101(31), 11197-11202
Åpne denne publikasjonen i ny fane eller vindu >>Twisting macromolecular chains: self-assembly of a chiral supermolecule from nonchiral polythiophene polyanions and random-coil synthetic peptides
2004 (engelsk)Inngår i: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 101, nr 31, s. 11197-11202Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The self-assembly of a negatively charged conjugated polythiophene derivative and a positively charged synthetic peptide will create a chiral, well ordered supermolecule. This supermolecule has the three-dimensional ordered structure of a biomolecule and the electronic properties of a conjugated polymer. The molecular complex being formed clearly affects the conformation of the polymer backbone. A main-chain chirality, such as a predominantly one-handed helical structure induced by the acid–base complexation between the conjugated polymer and the synthetic peptide, is seen. The alteration of the polymer backbone influences the optical properties of the polymer, seen as changes in the absorption, emission, and Raman spectra of the polymer. The complexation of the polythiophene and the synthetic peptide also induce a change from random-coil to helical structure of the synthetic peptide. The supermolecule described in this article may be used in a wide range of applications such as biomolecular devices, artificial enzymes, and biosensors.

HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-45666 (URN)10.1073/pnas.0401853101 (DOI)
Tilgjengelig fra: 2009-10-11 Laget: 2009-10-11 Sist oppdatert: 2017-12-13
Aili, D., Enander, K., Rydberg, J., Lundström, I., Baltzer, L. & Liedberg, B. (2003). Immobilization and heterodimerisation of helix-loop-helix polypeptides on gold surfaces - a model system for peptide-surface interactions. In: 1st World congress on Synthetic Receptors,2003.
Åpne denne publikasjonen i ny fane eller vindu >>Immobilization and heterodimerisation of helix-loop-helix polypeptides on gold surfaces - a model system for peptide-surface interactions
Vise andre…
2003 (engelsk)Inngår i: 1st World congress on Synthetic Receptors,2003, 2003Konferansepaper, Publicerat paper (Annet vitenskapelig)
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-42428 (URN)64002 (Lokal ID)64002 (Arkivnummer)64002 (OAI)
Tilgjengelig fra: 2009-10-10 Laget: 2009-10-10 Sist oppdatert: 2014-10-08
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