liu.seSearch for publications in DiVA
Change search
Link to record
Permanent link

Direct link
BETA
Rydberg, Johan
Alternative names
Publications (10 of 11) Show all publications
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
Open this publication in new window or tab >>Intrinsically unstructured proteins by designelectrostatic interactions can control binding, folding, and function of a helix-loop-helix heterodimer
2013 (English)In: Journal of Peptide Science, ISSN 1075-2617, E-ISSN 1099-1387, Vol. 19, no 8, p. 461-469Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
Wiley-Blackwell, 2013
Keywords
heterodimer, electrostatic interactions, folding, catalysis
National Category
Engineering and Technology
Identifiers
urn:nbn:se:liu:diva-95940 (URN)10.1002/psc.2520 (DOI)000321703200001 ()
Note

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

Available from: 2013-08-19 Created: 2013-08-12 Last updated: 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).
Open this publication in new window or tab >>Controlled Assembly of Gold Nanoparticles using De Novo Designed Polypeptide Scaffolds
Show others...
2008 (English)In: Proceedings SPIE, Vol. 6885, Photonic Biosensing and Microoptics, 2008, p. 688506-1-688506-8Conference paper, Published paper (Refereed)
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.

Keywords
Heterodimerization, polypeptides, gold nanoparticles, four-helix bundle, helix-loop-helix, self-assembly
National Category
Other Basic Medicine
Identifiers
urn:nbn:se:liu:diva-15118 (URN)10.1117/12.775806 (DOI)
Available from: 2008-10-16 Created: 2008-10-16 Last updated: 2018-01-12Bibliographically approved
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
Open this publication in new window or tab >>Folding Induced Assembly of Polypeptide Decorated Gold Nanoparticles
Show others...
2008 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 130, no 17, p. 5780-5788Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
ACS Publications, 2008
National Category
Other Basic Medicine
Identifiers
urn:nbn:se:liu:diva-15116 (URN)10.1021/ja711330f (DOI)
Available from: 2008-10-16 Created: 2008-10-16 Last updated: 2018-01-12Bibliographically approved
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
Open this publication in new window or tab >>Aggregation-Induced Folding of a de novo Designed Polypeptide Immobilized on Gold Nanoparticles
Show others...
2006 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 128, no 7, p. 2194 -2195Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
ACS Publications, 2006
Keywords
Not aviable
National Category
Other Basic Medicine
Identifiers
urn:nbn:se:liu:diva-14041 (URN)10.1021/ja057056j (DOI)
Available from: 2006-09-28 Created: 2006-09-28 Last updated: 2018-01-13Bibliographically approved
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.
Open this publication in new window or tab >>Intrinsically unstructured proteins by design: electrostatic interactions can control binding, folding and function of a helix-loop-helix heterodimer
2006 (English)Article in journal (Refereed) Submitted
National Category
Natural Sciences
Identifiers
urn:nbn:se:liu:diva-14038 (URN)
Available from: 2006-09-28 Created: 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
Open this publication in new window or tab >>Protein-protein interactions in model systems: design, control of catalytic activity and biosensor applications
2006 (English)Doctoral thesis, comprehensive summary (Other academic)
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.

Place, publisher, year, edition, pages
Linköping: Linköping University Electronic Press, 2006
Series
Linköping Studies in Science and Technology. Dissertations, ISSN 0345-7524 ; 1037
Keywords
Chemistry, Protein interactions, design, catalysis, biosensors, hybride materials, nanoparticles, Kemi
National Category
Chemical Sciences
Identifiers
urn:nbn:se:liu:diva-7485 (URN)91-85523-19-4 (ISBN)
Public defence
2006-09-22, Planck, Fysikhuset, Campus Valla, Linköpings universitet, Linköping, 09:15 (English)
Opponent
Supervisors
Available from: 2006-09-28 Created: 2006-09-28 Last updated: 2009-04-01Bibliographically approved
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.
Open this publication in new window or tab >>Alpha helix-inducing dimerization of synthetic polypeptide scaffolds on gold - a model system for receptor mimicking and biosensing
Show others...
2004 (English)In: 8th World Congress on Biosensors,2004, 2004Conference paper, Published paper (Other academic)
National Category
Natural Sciences
Identifiers
urn:nbn:se:liu:diva-42427 (URN)64001 (Local ID)64001 (Archive number)64001 (OAI)
Available from: 2009-10-10 Created: 2009-10-10 Last updated: 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.
Open this publication in new window or tab >>Folding-induced aggregation of polypeptide-decorated gold nanoparticles - an nano-scale Lego for the construction of complex hybrid materials
Show others...
2004 (English)In: 5th International Conference on Biological Physics,2004, 2004Conference paper, Published paper (Other academic)
National Category
Natural Sciences
Identifiers
urn:nbn:se:liu:diva-42426 (URN)64000 (Local ID)64000 (Archive number)64000 (OAI)
Available from: 2009-10-10 Created: 2009-10-10 Last updated: 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
Open this publication in new window or tab >>Twisting macromolecular chains: self-assembly of a chiral supermolecule from nonchiral polythiophene polyanions and random-coil synthetic peptides
2004 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 101, no 31, p. 11197-11202Article in journal (Refereed) 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.

National Category
Engineering and Technology
Identifiers
urn:nbn:se:liu:diva-45666 (URN)10.1073/pnas.0401853101 (DOI)
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 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.
Open this publication in new window or tab >>Immobilization and heterodimerisation of helix-loop-helix polypeptides on gold surfaces - a model system for peptide-surface interactions
Show others...
2003 (English)In: 1st World congress on Synthetic Receptors,2003, 2003Conference paper, Published paper (Other academic)
National Category
Natural Sciences
Identifiers
urn:nbn:se:liu:diva-42428 (URN)64002 (Local ID)64002 (Archive number)64002 (OAI)
Available from: 2009-10-10 Created: 2009-10-10 Last updated: 2014-10-08
Organisations

Search in DiVA

Show all publications