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http://purl.uniprot.org/citations/27463367http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27463367http://www.w3.org/2000/01/rdf-schema#comment"

Aim

To identify the shortest components of A13-A19, B12-B17 fragments capable for fibrillation and to validate the dependability of aggregation on the presence of hydroxyl group engaged in the 'tyrosine kissing'.

Materials & methods

Fragments A13-A19 and B12-B17 of insulin and all shortened analogues were obtained by using DMT/NMM/TosO(-) as a coupling reagent. The aggregation was studied by three independent tests.

Results

Studies on the susceptibility to aggregation of truncated analogs of insulin amyloidogenic core show three groups of peptides.

Conclusion

Truncation of A13-A419 fragment shows that fibrous structures are formed by all peptides bearing (13)H-LeuTyr-OH(14). Propensity to aggregation was found for (16)H-TyrLeu-OH(17) B12-B17 fragment. Tyrosine residue modification by incorporation of tert-butyl group on hydroxyl function gave analogues still predisposed to aggregation."xsd:string
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http://purl.uniprot.org/citations/27463367http://purl.uniprot.org/core/author"Wysocki S."xsd:string
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http://purl.uniprot.org/citations/27463367http://purl.uniprot.org/core/author"Galecki K."xsd:string
http://purl.uniprot.org/citations/27463367http://purl.uniprot.org/core/author"Kaminski Z.J."xsd:string
http://purl.uniprot.org/citations/27463367http://purl.uniprot.org/core/author"Kolesinska B."xsd:string
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http://purl.uniprot.org/citations/27463367http://purl.uniprot.org/core/author"R Dupont B.G."xsd:string
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http://purl.uniprot.org/citations/27463367http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27463367http://purl.uniprot.org/core/name"Nanomedicine (Lond)"xsd:string
http://purl.uniprot.org/citations/27463367http://purl.uniprot.org/core/pages"2083-2101"xsd:string
http://purl.uniprot.org/citations/27463367http://purl.uniprot.org/core/title"The quest for the shortest fragments of A (13-19) and B (12-17) responsible for the aggregation of human insulin."xsd:string
http://purl.uniprot.org/citations/27463367http://purl.uniprot.org/core/volume"11"xsd:string
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