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10.1038/ncomms8574 http://scihub22266oqcxt.onion/10.1038/ncomms8574 C4491812!4491812!26123690     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26123690&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2015 ; 6 (ä): ä Nephropedia Template TP {{tp|p=26123690|t=2015. Supramolecular amplification of amyloid self-assembly by iodination |pdf=|usr=}}{{26123690}} gab.com Text Supramolecular amplification of amyloid self-assembly by iodination JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26123690 #FOAvip 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 and without using organic solvents. Twit Text FOAVip Supramolecular amplification of amyloid self-assembly by iodination ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26123690 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26123690 #FOAvip English Wikipedia <ref>{{Cite pmid|26123690}}</ref> Supramolecular amplification of amyloid self-assembly by iodination #MMPMID26123690 Bertolani A; Pirrie L; Stefan L; Houbenov N; Haataja JS; Catalano L; Terraneo G; Giancane G; Valli L; Milani R; Ikkala O; Resnati G; Metrangolo P Nat Commun 2015[]; 6 (ä): ä PMID26123690show ga 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 and without using organic solvents. äSupramolecular amplification of amyloid self-assembly by iodination (epmc).pdf DeepDyve Pubget Overpricing