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Publications (10 of 21) Show all publications
Chaudhary, H., Ferreira Fernandes, R. M., Gowda, V., Claessens, M. M. A., Furo, I. & Lendel, C. (2019). Intrinsically disordered protein as carbon nanotube dispersant: How dynamic interactions lead to excellent colloidal stability. Journal of Colloid and Interface Science, 556, 172-179
Open this publication in new window or tab >>Intrinsically disordered protein as carbon nanotube dispersant: How dynamic interactions lead to excellent colloidal stability
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2019 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 556, p. 172-179Article in journal (Refereed) Published
Abstract [en]

The rich pool of protein conformations combined with the dimensions and properties of carbon nanotubes create new possibilities in functional materials and nanomedicine. Here, the intrinsically disordered protein α-synuclein is explored as a dispersant of single-walled carbon nanotubes (SWNTs) in water. We use a range of spectroscopic methods to quantify the amount of dispersed SWNT and to elucidate the binding mode of α-synuclein to SWNT. The dispersion ability of α-synuclein is good even with mild sonication and the obtained dispersion is very stable over time. The whole polypeptide chain is involved in the interaction accompanied by a fraction of the chain changing into a helical structure upon binding. Similar to other dispersants, we observe that only a small fraction (15–20%) of α-synuclein is adsorbed on the SWNT surface with an average residence time below 10 ms

Place, publisher, year, edition, pages
Academic Press, 2019
National Category
Physical Chemistry
Identifiers
urn:nbn:se:kth:diva-258234 (URN)10.1016/j.jcis.2019.08.050 (DOI)2-s2.0-85070901886 (Scopus ID)
Note

QC 20191014

Available from: 2019-09-10 Created: 2019-09-10 Last updated: 2019-10-15Bibliographically approved
Atapour, M., Wei, Z., Chaudhary, H., Lendel, C., Odnevall Wallinder, I. & Hedberg, Y. (2019). Metal release from stainless steel 316L in whey protein - And simulated milk solutions under static and stirring conditions. Food Control, 101, 163-172
Open this publication in new window or tab >>Metal release from stainless steel 316L in whey protein - And simulated milk solutions under static and stirring conditions
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2019 (English)In: Food Control, ISSN 0956-7135, E-ISSN 1873-7129, Vol. 101, p. 163-172Article in journal (Refereed) Published
Abstract [en]

Stainless steel is an important transport and processing contact material for bovine milk and dairy products. Release (migration) of metals, ions, complexes or wear debris/particles, and metal-induced protein aggregation in such environments are hence important to consider both from a corrosion and food safety perspective. This study aims on investigating the release of iron (Fe), chromium (Cr), and nickel (Ni) from AISI 316L stainless steel in contact with whey protein solutions relevant for protein drinks, and on how the whey proteins are influenced by stirring with a magnetic stir bar and metal release. Mechanistic insight is gained by parallel investigations of metal release from two reference non-protein containing solutions, a metal-complexing (citrate-containing) simulated milk solution (SMS) and a low complexing phosphate buffered saline solution (PBS). All immersion exposures were conducted at pH 6.8 for 0.5, 4, 24 and 48 hat room temperature at static and stirring conditions. All solutions and samples were investigated using different chemical, spectroscopic, microscopic, and electrochemical methods. Significantly higher amounts of Fe, Cr, and Ni were released into the whey protein solution (80 g/L) as compared to SMS and PBS. Strong enrichment of Cr in the surface oxide and reduction of the surface oxide thickness were associated with a higher amount of Ni release in the metal-complexing solutions (SMS and whey protein) compared with PBS. Stirring conditions resulted in higher amounts of metal release, enrichment of Cr in the surface oxide, and clear signs of wear of the 316L surface in all solutions compared to static conditions. The wear mechanism in the whey protein solution was different as compared to corresponding processes in SMS and PBS, involving an etching-like process and larger-sized wear debris. Electrochemical measurements at static conditions confirmed observed differences between the solutions, with the lowest corrosion resistance observed for coupons exposed in the whey protein solution, followed by SMS and PBS. Released metals in solution from the 316L coupons in contact with the whey protein solution resulted in enhanced rates of protein aggregation and precipitation of protein aggregates from solution. Further studies should be made to investigate other relevant test conditions and assess toxicological risks.

Place, publisher, year, edition, pages
ELSEVIER SCI LTD, 2019
Keywords
Protein, Whey, Stainless steel, Metal release, Food, Milk, Atomic absorption spectroscopy, X-ray photoelectron spectroscopy, Photon cross correlation spectroscopy, UV- visible spectroscopy, Scanning electron microscopy, Polarization resistance, Corrosion
National Category
Corrosion Engineering
Identifiers
urn:nbn:se:kth:diva-251269 (URN)10.1016/j.foodcont.2019.02.031 (DOI)000465049000023 ()2-s2.0-85063112841 (Scopus ID)
Note

QC 20190513

Available from: 2019-05-13 Created: 2019-05-13 Last updated: 2019-05-29Bibliographically approved
Ye, X., Lendel, C., Langton, M., Olsson, R. & Hedenqvist, M. S. (2019). Protein nanofibrils: Preparation, properties, and possible applications in industrial nanomaterials. In: Industrial Applications of Nanomaterials: (pp. 29-63). Elsevier
Open this publication in new window or tab >>Protein nanofibrils: Preparation, properties, and possible applications in industrial nanomaterials
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2019 (English)In: Industrial Applications of Nanomaterials, Elsevier, 2019, p. 29-63Chapter in book (Other academic)
Abstract [en]

This chapter deals with protein nanofibrils (PNFs), also referred to as amyloid fibrils. This is an emerging field in nanoscience and engineering. Sources for PNFs, ways of making these, including the mechanisms of the fibrillation process, and factors affecting the production process are presented here. Properties of the PNFs themselves as well as properties and preparation of PNF materials in the form of hydrogels, films, and fibers are also described. In this chapter, PNF-based nanocomposites and templates are also considered. Possible applications of PNFs are discussed and put in the perspective of future uses as, or in, industrial nanomaterials.

Place, publisher, year, edition, pages
Elsevier, 2019
National Category
Materials Chemistry
Identifiers
urn:nbn:se:kth:diva-258235 (URN)10.1016/B978-0-12-815749-7.00002-5 (DOI)978-0-12-815749-7 (ISBN)
Note

QC 20191015

Available from: 2019-09-10 Created: 2019-09-10 Last updated: 2019-10-15Bibliographically approved
Josefsson, L., Cronhamn, M., Ekman, M., Widehammar, H., Emmer, Å. & Lendel, C. (2019). Structural basis for the formation of soy protein nanofibrils. RSC Advances, 9(11), 6310-6319
Open this publication in new window or tab >>Structural basis for the formation of soy protein nanofibrils
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2019 (English)In: RSC Advances, ISSN 2046-2069, E-ISSN 2046-2069, Vol. 9, no 11, p. 6310-6319Article in journal (Refereed) Published
Abstract [en]

Amyloid-like protein nanofibrils (PNFs) can assemble from a range of different proteins including disease-associated proteins, functional amyloid proteins and several proteins for which the PNFs are neither related to disease nor function. We here examined the core building blocks of PNFs formed by soy proteins. Fibril formation at pH 2 and 90 degrees C is coupled to peptide hydrolysis which allows isolation of the PNF-forming peptides and identification of them by mass spectrometry. We found five peptides that constitute the main building blocks in soy PNFs, three of them from the protein b-conglycinin and two from the protein glycinin. The abilities of these peptides to form PNFs were addressed by amyloid prediction software and by PNF formation of the corresponding synthetic peptides. Analysis of the structural context in the native soy proteins revealed two structural motifs for the PNF-forming peptides: (i) so-called b-arches and (ii) helical segments involved in quaternary structure contacts. However, the results suggest that neither the native structural motifs nor the protein of origin defines the morphology of the PNFs formed from soy protein isolate.

Place, publisher, year, edition, pages
ROYAL SOC CHEMISTRY, 2019
National Category
Physical Chemistry
Identifiers
urn:nbn:se:kth:diva-246262 (URN)10.1039/c8ra10610j (DOI)000459507800054 ()2-s2.0-85062456643 (Scopus ID)
Note

QC 20190326

Available from: 2019-03-26 Created: 2019-03-26 Last updated: 2019-09-18Bibliographically approved
Hedberg, Y., Dobryden, I., Chaudhary, H., Wei, Z., Claesson, P. M. & Lendel, C. (2019). Synergistic effects of metal-induced aggregation of human serum albumin. Colloids and Surfaces B: Biointerfaces, 173, 751-758
Open this publication in new window or tab >>Synergistic effects of metal-induced aggregation of human serum albumin
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2019 (English)In: Colloids and Surfaces B: Biointerfaces, ISSN 0927-7765, E-ISSN 1873-4367, Vol. 173, p. 751-758Article in journal (Refereed) Published
Abstract [en]

Exposure to cobalt (Co), chromium (Cr), and nickel (Ni) occurs often via skin contact and from different dental and orthopedic implants. The metal ions bind to proteins, which may induce structural changes and aggregation, with different medical consequences. We investigated human serum albumin (HSA) aggregation in the presence of Co-II, Cr-III, and/or Ni-II ions and/or their nanoparticle precipitates by using scattering, spectroscopic, and imaging techniques, at simulated physiological conditions (phosphate buffered saline - PBS, pH 7.3) using metal salts that did not affect the pH, and at HSA:metal molar ratios of up to 1:8. Co ions formed some solid nano particles in PBS at the investigated conditions, as determined by nanoparticle tracking analysis, but the Cr-III anions and Ni-II ions remained fully soluble. It was found that all metal ions induced HSA aggregation, and this effect was significantly enhanced when a mixture of all three metal ions was present instead of any single type of ion. Thus, the metal ions induce aggregation synergistically. HSA aggregates formed linear structures on a mica surface in the presence of Cr-III ions. A clear tendency of aggregation and linearly aligned aggregates was seen in the presence of all three metal ions. Spectroscopic investigations indicated that the majority of the HSA molecules maintained their alpha helical secondary structure and conformation. This study highlights the importance of synergistic effects of metal ions and/or their precipitates on protein aggregation, which are highly relevant for implant materials and common exposures to metals.

Place, publisher, year, edition, pages
ELSEVIER SCIENCE BV, 2019
Keywords
Cobalt, Chromium, Nickel, Binding, Albumin, Aggregation
National Category
Physical Chemistry
Identifiers
urn:nbn:se:kth:diva-241193 (URN)10.1016/j.colsurfb.2018.10.061 (DOI)000454377300089 ()30384272 (PubMedID)2-s2.0-85055579350 (Scopus ID)
Note

QC 20190121

Available from: 2019-01-21 Created: 2019-01-21 Last updated: 2019-01-21Bibliographically approved
Almandoz-Gil, L., Welander, H., Ihse, E., Khoonsari, P. E., Musunuri, S., Lendel, C., . . . Bergstrom, J. (2018). Low molar excess of 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote oligomerization of alpha-synuclein through different pathways (vol 110, pg 421, 2017). Free Radical Biology & Medicine, 117, 258-258
Open this publication in new window or tab >>Low molar excess of 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote oligomerization of alpha-synuclein through different pathways (vol 110, pg 421, 2017)
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2018 (English)In: Free Radical Biology & Medicine, ISSN 0891-5849, E-ISSN 1873-4596, Vol. 117, p. 258-258Article in journal (Refereed) Published
Place, publisher, year, edition, pages
ELSEVIER SCIENCE INC, 2018
National Category
Biological Sciences
Identifiers
urn:nbn:se:kth:diva-225742 (URN)10.1016/j.freeradbiomed.2018.02.007 (DOI)000427420600025 ()29455934 (PubMedID)2-s2.0-85042050328 (Scopus ID)
Note

QC 20180410

Available from: 2018-04-10 Created: 2018-04-10 Last updated: 2018-04-10Bibliographically approved
Ye, X., Hedenqvist, M. S., Langton, M. & Lendel, C. (2018). On the role of peptide hydrolysis for fibrillation kinetics and amyloid fibril morphology. RSC Advances, 8(13), 6915-6924
Open this publication in new window or tab >>On the role of peptide hydrolysis for fibrillation kinetics and amyloid fibril morphology
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
National Category
Chemical Sciences
Identifiers
urn:nbn:se:kth:diva-224069 (URN)10.1039/c7ra10981d (DOI)000425508900022 ()2-s2.0-85042187152 (Scopus ID)
Note

QC 20180314

Available from: 2018-03-14 Created: 2018-03-14 Last updated: 2018-03-14Bibliographically approved
Ye, X., Junel, K., Gallstedt, M., Langton, M., Wei, X.-F., Lendel, C. & Hedenqvist, M. S. (2018). Protein/Protein Nanocomposite Based on Whey Protein Nanofibrils in a Whey Protein Matrix. ACS Sustainable Chemistry and Engineering, 6(4), 5462-5469
Open this publication in new window or tab >>Protein/Protein Nanocomposite Based on Whey Protein Nanofibrils in a Whey Protein Matrix
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2018 (English)In: ACS Sustainable Chemistry and Engineering, ISSN 2168-0485, Vol. 6, no 4, p. 5462-5469Article in journal (Refereed) Published
Abstract [en]

This article describes nanocomposite films with separately grown protein nanofibrils (PNFs) in a nonfibrillar protein matrix from the same protein starting material (whey). Tensile tests on the glycerol-plasticized films indicate an increased elastic modulus and a decreased extensibility with increasing content of PNFs, although the films are still ductile at the maximum PNF content (15 wt %). Infrared spectroscopy confirms that the strongly hydrogen-bonded beta-sheets in the PNFs are retained in the composites. The films appear with a PNF-induced undulated upper surface. It is shown that micrometer-scale spatial variations in the glycerol distribution are not the cause of these undulations. Instead, the undulations seem to be a feature of the PNF material itself. It was also shown that, apart from plasticizing the protein film, the presence of glycerol seemed to favor to some extent exfoliation of stacked beta-sheets in the proteins, as revealed by X-ray diffraction.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2018
Keywords
Protein fibrils, Whey, Nanocomposite, Protein structure, Mechanical properties
National Category
Chemical Sciences
Identifiers
urn:nbn:se:kth:diva-226781 (URN)10.1021/acssuschemeng.8b00330 (DOI)000429285800111 ()2-s2.0-85044728815 (Scopus ID)
Funder
Swedish Research Council Formas, 213-2014-1389
Note

QC 20180507

Available from: 2018-05-07 Created: 2018-05-07 Last updated: 2019-10-09Bibliographically approved
Almandoz-Gil, L., Welander, H., Ihse, E., Khoonsari, P. E., Musunuri, S., Lendel, C., . . . Bergstrom, J. (2017). Low molar excess of 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote oligomerization of alpha-synuclein through different pathways. Free Radical Biology & Medicine, 110, 421-431
Open this publication in new window or tab >>Low molar excess of 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote oligomerization of alpha-synuclein through different pathways
Show others...
2017 (English)In: Free Radical Biology & Medicine, ISSN 0891-5849, E-ISSN 1873-4596, Vol. 110, p. 421-431Article in journal (Refereed) Published
Abstract [en]

Aggregated alpha-synuclein is the main component of Lewy bodies, intraneuronal inclusions found in brains with Parkinson's disease and dementia with Lewy bodies. A body of evidence implicates oxidative stress in the pathogenesis of these diseases. For example, a large excess (30: 1, aldehyde: protein) of the lipid peroxidation end products 4-oxo-2-nonenal (ONE) or 4-hydroxy-2-nonenal (HNE) can induce alpha-synuclein oligomer formation. The objective of the study was to investigate the effect of these reactive aldehydes on alpha-synuclein at a lower molar excess (3: 1) at both physiological (7.4) and acidic (5.4) pH. As observed by size-exclusion chromatography, ONE rapidly induced the formation of alpha-synuclein oligomers at both pH values, but the effect was less pronounced under the acidic condition. In contrast, only a small proportion of alpha-synuclein oligomers were formed with low excess HNE-treatment at physiological pH and no oligomers at all under the acidic condition. With prolonged incubation times (up to 96 h), more alpha-synuclein was oligomerized at physiological pH for both ONE and HNE. As determined by Western blot, ONE-oligomers were more SDS-stable and to a higher-degree cross-linked as compared to the HNE-induced oligomers. However, as shown by their greater sensitivity to proteinase K treatment, ONE-oligomers, exhibited a less compact structure than HNE-oligomers. As indicated by mass spectrometry, ONE modified most Lys residues, whereas HNE primarily modified the His50 residue and fewer Lys residues, albeit to a higher degree than ONE. Taken together, our data show that the aldehydes ONE and HNE can modify alpha-synuclein and induce oligomerization, even at low molar excess, but to a higher degree at physiological pH and seemingly through different pathways.

Place, publisher, year, edition, pages
Elsevier, 2017
Keywords
Alpha-synuclein, Oligomers, 4-oxo-2-nonenal, 4-hydroxy-2-nonenal, Oxidative stress
National Category
Biological Sciences
Identifiers
urn:nbn:se:kth:diva-211583 (URN)10.1016/j.freeradbiomed.2017.07.004 (DOI)000406049200038 ()2-s2.0-85023184492 (Scopus ID)
Funder
Swedish Research Council, 2011-4519Swedish Research Council, 2012-2172Swedish Research Council, 2010-6745Marianne and Marcus Wallenberg FoundationThe Swedish Brain FoundationSwedish Society for Medical Research (SSMF)Åke Wiberg Foundation
Note

QC 20170815

Available from: 2017-08-15 Created: 2017-08-15 Last updated: 2017-08-15Bibliographically approved
Kamada, A., Mittal, N., Söderberg, D., Lendel, C. & Lundell, F. (2016). Assembly mechanism of nanostructured whey protein filaments. Abstracts of Papers of the American Chemical Society, 252
Open this publication in new window or tab >>Assembly mechanism of nanostructured whey protein filaments
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2016 (English)In: Abstracts of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 252Article in journal, Meeting abstract (Other academic) Published
Place, publisher, year, edition, pages
AMER CHEMICAL SOC, 2016
National Category
Organic Chemistry
Identifiers
urn:nbn:se:kth:diva-242627 (URN)000431460402815 ()
Note

QC 20190225

Available from: 2019-02-25 Created: 2019-02-25 Last updated: 2019-08-21Bibliographically approved
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0001-9238-7246

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