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On the role of peptide hydrolysis for fibrillation kinetics and amyloid fibril morphology
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Applied Physical Chemistry.ORCID iD: 0000-0001-9238-7246
2018 (English)In: RSC Advances, ISSN 2046-2069, E-ISSN 2046-2069, Vol. 8, no 13, p. 6915-6924Article in journal (Refereed) Published
Abstract [en]

Self-assembly of proteins into amyloid-like nanofibrils is not only a key event in several diseases, but such fibrils are also associated with intriguing biological function and constitute promising components for new biobased materials. The bovine whey protein beta-lactoglobulin has emerged as an important model protein for the development of such materials. We here report that peptide hydrolysis is the rate-determining step for fibrillation of beta-lactoglobulin in whey protein isolate. We also explore the observation that beta-lactoglobulin nanofibrils of distinct morphologies are obtained by simply changing the initial protein concentration. We find that the morphological switch is related to different nucleation mechanisms and that the two classes of nanofibrils are associated with variations of the peptide building blocks. Based on the results, we propose that the balance between protein concentration and the hydrolysis rate determines the structure of the formed nanofibrils.

Place, publisher, year, edition, pages
ROYAL SOC CHEMISTRY , 2018. Vol. 8, no 13, p. 6915-6924
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Chemical Sciences
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URN: urn:nbn:se:kth:diva-224069DOI: 10.1039/c7ra10981dISI: 000425508900022Scopus ID: 2-s2.0-85042187152OAI: oai:DiVA.org:kth-224069DiVA, id: diva2:1190504
Note

QC 20180314

Available from: 2018-03-14 Created: 2018-03-14 Last updated: 2018-03-14Bibliographically approved

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Hedenqvist, Mikael S.Lendel, Christofer

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