Supramolecular amplification of amyloid self-assembly by iodination

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dc.contributor Aalto-yliopisto fi
dc.contributor Aalto University en
dc.contributor.author Bertolani, Arianna
dc.contributor.author Pirrie, Lisa
dc.contributor.author Stefan, Loic
dc.contributor.author Houbenov, Nikolay
dc.contributor.author Haataja, Johannes S.
dc.contributor.author Catalano, Luca
dc.contributor.author Terraneo, Giancarlo
dc.contributor.author Giancane, Gabriele
dc.contributor.author Valli, Ludovico
dc.contributor.author Milani, Roberto
dc.contributor.author Ikkala, Olli
dc.contributor.author Resnati, Giuseppe
dc.contributor.author Metrangolo, Pierangelo
dc.date.accessioned 2017-05-11T08:25:43Z
dc.date.available 2017-05-11T08:25:43Z
dc.date.issued 2015
dc.identifier.citation Bertolani , A , Pirrie , L , Stefan , L , Houbenov , N , Haataja , J S , Catalano , L , Terraneo , G , Giancane , G , Valli , L , Milani , R , Ikkala , O , Resnati , G & Metrangolo , P 2015 , ' Supramolecular amplification of amyloid self-assembly by iodination ' NATURE COMMUNICATIONS , vol 6 , 7574 , pp. 1-9 . DOI: 10.1038/ncomms8574 en
dc.identifier.issn 2041-1723
dc.identifier.other PURE UUID: 71e093db-02b1-4be5-a992-dc121c739c51
dc.identifier.other PURE ITEMURL: https://research.aalto.fi/en/publications/supramolecular-amplification-of-amyloid-selfassembly-by-iodination(71e093db-02b1-4be5-a992-dc121c739c51).html
dc.identifier.other PURE FILEURL: https://research.aalto.fi/files/12948462/ncomms8574.pdf
dc.identifier.uri https://aaltodoc.aalto.fi/handle/123456789/25608
dc.description.abstract Amyloid supramolecular assemblies have found widespread exploitation as ordered nanomaterials in a range of applications from materials science to biotechnology. New strategies are, however, required for understanding and promoting mature fibril formation from simple monomer motifs through easy and scalable processes. Noncovalent interactions are key to forming and holding the amyloid structure together. On the other hand, the halogen bond has never been used purposefully to achieve control over amyloid self-assembly. Here we show that single atom replacement of hydrogen with iodine, a halogen-bond donor, in the human calcitonin-derived amyloidogenic fragment DFNKF results in a super-gelator peptide, which forms a strong and shape-persistent hydrogel at 30-fold lower concentration than the wild-type pentapeptide. This is remarkable for such a modest perturbation in structure. Iodination of aromatic amino acids may thus develop as a general strategy for the design of new hydrogels from unprotected peptides andwithout using organic solvents. en
dc.format.extent 1-9
dc.format.mimetype application/pdf
dc.language.iso en en
dc.relation.ispartofseries NATURE COMMUNICATIONS en
dc.relation.ispartofseries Volume 6 en
dc.rights openAccess en
dc.subject.other 114 Physical sciences en
dc.subject.other 221 Nanotechnology en
dc.subject.other 214 Mechanical engineering en
dc.subject.other 218 Environmental engineering en
dc.title Supramolecular amplification of amyloid self-assembly by iodination en
dc.type A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä fi
dc.description.version Peer reviewed en
dc.contributor.department Department of Applied Physics en
dc.subject.keyword amyloid
dc.subject.keyword 114 Physical sciences
dc.subject.keyword 221 Nanotechnology
dc.subject.keyword 214 Mechanical engineering
dc.subject.keyword 218 Environmental engineering
dc.identifier.urn URN:NBN:fi:aalto-201705113992
dc.identifier.doi 10.1038/ncomms8574
dc.type.version publishedVersion


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