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Davoodi, S., Ornithopoulou, E., J. Gavillet, C., Davydok, A., Roth, S. V., Lendel, C. & Lundell, F. (2025). Confinement induced self-assembly of protein nanofibrils probed by microfocus X-ray scattering. Journal of Physical Chemistry B, 129(3), 1070-1081
Open this publication in new window or tab >>Confinement induced self-assembly of protein nanofibrils probed by microfocus X-ray scattering
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2025 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 129, no 3, p. 1070-1081Article in journal (Refereed) Published
Abstract [en]

We here explore confinement-induced assembly of whey protein nanofibrils (PNFs) into microscale fibers using micro-focused synchrotron X-ray scattering. Solvent evaporation aligns the PNFs into anisotropic fibers and the process is followed in situ by scattering experiments in a droplet of PNF dispersion. We find an optimal temperature at which the order of the protein fiber has a maximum, suggesting that the degree of order results from a balance between the time scales of the forced alignment and the rotational diffusion of the fibrils. Moreover, we observe that the assembly process depends on the nano-scale morphology of the PNFs. Stiff PNFs with a persistence length in the micrometer scale are aligned at the air-water interface and the anisotropy gradually decrease towards the center of the droplet. Marangoni flows often increase entanglements toward the center, leading to complex patterns in the droplet. Flexible fibrils with a short persistence length (< 100 nm) tends to align uniformly throughout the droplet, possibly due to stronger local entanglements. Straight PNFs form smaller clusters with shorter inter-cluster distances due to their tight packing and consistent linear structure. In contrast, curved PNFs form intricate networks with larger characteristic distances and more varied structures because of their flexibility and adaptability.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2025
National Category
Fluid Mechanics Structural Biology Physical Chemistry Other Physics Topics
Research subject
Biotechnology; Physics, Material and Nano Physics
Identifiers
urn:nbn:se:kth:diva-354251 (URN)10.1021/acs.jpcb.4c04386 (DOI)001398066100001 ()39808180 (PubMedID)2-s2.0-85215848590 (Scopus ID)
Note

QC 20250225

Available from: 2024-10-02 Created: 2024-10-02 Last updated: 2025-02-25Bibliographically approved
Pires, R. S., Capezza, A. J., Johansson, M., Langton, M. & Lendel, C. (2025). Seed-induced gelation of whey protein via fibril elongation amplification. Food Hydrocolloids, 167, Article ID 111424.
Open this publication in new window or tab >>Seed-induced gelation of whey protein via fibril elongation amplification
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2025 (English)In: Food Hydrocolloids, ISSN 0268-005X, E-ISSN 1873-7137, Vol. 167, article id 111424Article in journal (Refereed) Published
Abstract [en]

Protein nanofibrils (PNFs), especially those from the whey protein β-lactoglobulin, hold the promise for applications in food technology, medicine, and sustainable materials. In this work, we explore the mechanisms underlying the sol-gel transition of whey protein isolate triggered by pre-fragmented whey fibrils (seeds) at low pH and high temperature. We show that, under these conditions, the formed hydrogels are constructed from PNFs. The presented results suggest that the seeds amplify the fibril growth process by providing active ends that capture peptide monomers produced via acid hydrolysis. This changes the fibrils' length distribution (up to 10-fold increase of their average contour length), and the samples reach the percolation threshold at a much lower mass concentration of fibrils. We also note that seeding has a strong impact on morphology and catalyzes a conversion of short, curved fibrils into long straight ones, which also contribute to the lower percolation limit. Rheological measurements indicate that attractive inter-fibrillar forces stabilize the PNF network. This is further evidenced by the gels’ resistance to disassembly across a wide pH range, implying that other forces than electrostatics are important for stabilizing the fibrillar network. Finally, we discuss the nature of the sol-gel transition based on continuum percolation theory, which corroborates the observed relationship between PNF length distribution and the sol-gel transition.

Place, publisher, year, edition, pages
Elsevier BV, 2025
Keywords
Hydrogel, Percolation, Protein nanofibrils, Seeding, Sol-gel transition, Whey protein
National Category
Physical Chemistry
Identifiers
urn:nbn:se:kth:diva-362714 (URN)10.1016/j.foodhyd.2025.111424 (DOI)001475268400001 ()2-s2.0-105002643194 (Scopus ID)
Note

QC 20250609

Available from: 2025-04-23 Created: 2025-04-23 Last updated: 2025-06-09Bibliographically approved
De Oliveira, D. H., Gowda, V., Sparrman, T., Gustafsson, L., Pires, R. S., Riekel, C., . . . Hedhammar, M. (2024). Structural conversion of the spidroin C-terminal domain during assembly of spider silk fibers. Nature Communications, 15(1), Article ID 4670.
Open this publication in new window or tab >>Structural conversion of the spidroin C-terminal domain during assembly of spider silk fibers
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2024 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 15, no 1, article id 4670Article in journal (Refereed) Published
Abstract [en]

The major ampullate Spidroin 1 (MaSp1) is the main protein of the dragline spider silk. The C-terminal (CT) domain of MaSp1 is crucial for the self-assembly into fibers but the details of how it contributes to the fiber formation remain unsolved. Here we exploit the fact that the CT domain can form silk-like fibers by itself to gain knowledge about this transition. Structural investigations of fibers from recombinantly produced CT domain from E. australis MaSp1 reveal an α-helix to β-sheet transition upon fiber formation and highlight the helix No4 segment as most likely to initiate the structural conversion. This prediction is corroborated by the finding that a peptide corresponding to helix No4 has the ability of pH-induced conversion into β-sheets and self-assembly into nanofibrils. Our results provide structural information about the CT domain in fiber form and clues about its role in triggering the structural conversion of spidroins during fiber assembly.

Place, publisher, year, edition, pages
Springer Nature, 2024
National Category
Structural Biology
Identifiers
urn:nbn:se:kth:diva-347634 (URN)10.1038/s41467-024-49111-5 (DOI)001236598600033 ()38821983 (PubMedID)2-s2.0-85195000928 (Scopus ID)
Note

QC 20240613

Available from: 2024-06-12 Created: 2024-06-12 Last updated: 2024-07-05Bibliographically approved
Proietti, G., Axelsson, A., Capezza, A. J., Todarwal, Y., Kuzmin, J., Linares, M., . . . Dinér, P. (2024). Ultralight aerogels via supramolecular polymerization of a new chiral perfluoropyridine-based sulfonimidamide organogelator. Nanoscale, 16(15), 7603-7611
Open this publication in new window or tab >>Ultralight aerogels via supramolecular polymerization of a new chiral perfluoropyridine-based sulfonimidamide organogelator
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2024 (English)In: Nanoscale, ISSN 2040-3364, E-ISSN 2040-3372, Vol. 16, no 15, p. 7603-7611Article in journal (Refereed) Published
Abstract [en]

Chiral and enantiopure perfluorinated sulfonimidamides act as low-molecular weight gelators at low critical gelation concentration (<1 mg mL-1) via supramolecular polymerization in nonpolar organic solvents and more heterogenic mixtures, such as biodiesel and oil. Freeze-drying of the organogel leads to ultralight aerogel with extremely low density (1 mg mL-1). The gelation is driven by hydrogen bonding resulting in a helical molecular ordering and unique fibre assemblies as confirmed by scanning electron microscopy, CD spectroscopy, and computational modeling of the supramolecular structure.

Place, publisher, year, edition, pages
Royal Society of Chemistry (RSC), 2024
National Category
Chemical Sciences
Research subject
Chemistry
Identifiers
urn:nbn:se:kth:diva-347069 (URN)10.1039/d3nr06460c (DOI)001188638600001 ()38512219 (PubMedID)2-s2.0-85188741705 (Scopus ID)
Funder
Carl Tryggers foundation , CTS:19-80Swedish Research Council, 2023-04482Swedish Research Council, 2023-5171Bo Rydin Foundation for Scientific Research, F 30/19Carl Tryggers foundation , CTS:19-80Swedish Research Council, 2023-04482Swedish Research Council, 2023-5171Bo Rydin Foundation for Scientific Research, F 30/19
Note

QC 20240603

Available from: 2024-05-31 Created: 2024-05-31 Last updated: 2024-06-03Bibliographically approved
Pires, R. S. & Lendel, C. (2023). Controlling the assembly of protein nanofibril hydrogels. European Biophysics Journal, 52(SUPPL 1), S205-S205
Open this publication in new window or tab >>Controlling the assembly of protein nanofibril hydrogels
2023 (English)In: European Biophysics Journal, ISSN 0175-7571, E-ISSN 1432-1017, Vol. 52, no SUPPL 1, p. S205-S205Article in journal, Meeting abstract (Other academic) Published
Place, publisher, year, edition, pages
SPRINGER, 2023
National Category
Biophysics
Identifiers
urn:nbn:se:kth:diva-335942 (URN)001029235400713 ()
Note

QC 20230911

Available from: 2023-09-11 Created: 2023-09-11 Last updated: 2025-02-20Bibliographically approved
Lendel, C., Hedenqvist, M. S., Langton, M. & Lundell, F. (2023). Design of hierarchical protein materials for a sustainable society. European Biophysics Journal, 52(SUPPL 1), S48-S48
Open this publication in new window or tab >>Design of hierarchical protein materials for a sustainable society
2023 (English)In: European Biophysics Journal, ISSN 0175-7571, E-ISSN 1432-1017, Vol. 52, no SUPPL 1, p. S48-S48Article in journal, Meeting abstract (Other academic) Published
Place, publisher, year, edition, pages
SPRINGER, 2023
National Category
Textile, Rubber and Polymeric Materials
Identifiers
urn:nbn:se:kth:diva-335875 (URN)001029235400103 ()
Note

QC 20230911

Available from: 2023-09-11 Created: 2023-09-11 Last updated: 2023-09-11Bibliographically approved
Rahman, M. M., Pires, R. S., Herneke, A., Gowda, V., Langton, M., Biverstal, H. & Lendel, C. (2023). Food protein-derived amyloids do not accelerate amyloid beta aggregation. Scientific Reports, 13(1)
Open this publication in new window or tab >>Food protein-derived amyloids do not accelerate amyloid beta aggregation
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2023 (English)In: Scientific Reports, E-ISSN 2045-2322, Vol. 13, no 1Article in journal (Refereed) Published
Abstract [en]

The deposition of proteins in the form of amyloid fibrils is closely associated with several serious diseases. The events that trigger the conversion from soluble functional proteins into insoluble amyloid are not fully understood. Many proteins that are not associated with disease can form amyloid with similar structural characteristics as the disease-associated fibrils, which highlights the potential risk of cross-seeding of disease amyloid by amyloid-like structures encountered in our surrounding. Of particular interest are common food proteins that can be transformed into amyloid under conditions similar to cooking. We here investigate cross-seeding of amyloid-beta (A beta), a peptide known to form amyloid during the development of Alzheimer's disease, by 16 types of amyloid fibrils derived from food proteins or peptides. Kinetic studies using thioflavin T fluorescence as output show that none of the investigated protein fibrils accelerates the aggregation of A beta. In at least two cases (hen egg lysozyme and oat protein isolate) we observe retardation of the aggregation, which appears to originate from interactions between the food protein seeds and A beta in aggregated form. The results support the view that food-derived amyloid is not a risk factor for development of A beta pathology and Alzheimer's disease.

Place, publisher, year, edition, pages
Springer Nature, 2023
National Category
Biochemistry Molecular Biology
Identifiers
urn:nbn:se:kth:diva-329450 (URN)10.1038/s41598-023-28147-5 (DOI)000985232500054 ()36720893 (PubMedID)2-s2.0-85147104197 (Scopus ID)
Note

QC 20230621

Available from: 2023-06-21 Created: 2023-06-21 Last updated: 2025-02-20Bibliographically approved
Herneke, A., Lendel, C., Karkehabadi, S., Lu, J. & Langton, M. (2023). Protein Nanofibrils from Fava Bean and Its Major Storage Proteins: Formation and Ability to Generate and Stabilise Foams. Foods, 12(3), Article ID 521.
Open this publication in new window or tab >>Protein Nanofibrils from Fava Bean and Its Major Storage Proteins: Formation and Ability to Generate and Stabilise Foams
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2023 (English)In: Foods, E-ISSN 2304-8158, Vol. 12, no 3, article id 521Article in journal (Refereed) Published
Abstract [en]

Protein nanofibrils (PNFs) have potential for use in food applications as texture inducers. This study investigated the formation of PNFs from protein extracted from whole fava bean and from its two major storage proteins, globulin fractions 11S and 7S. PNFs were formed by heating (85 degrees C) the proteins under acidic conditions (pH 2) for 24 h. Thioflavin T fluorescence and atomic force microscopy techniques were used to investigate PNF formation. The foaming properties (capacity, stability, and half-life) were explored for non-fibrillated and fibrillated protein from fava bean, 11S, and 7S to investigate the texturing ability of PNFs at concentrations of 1 and 10 mg/mL and pH 7. The results showed that all three heat-incubated proteins (fava bean, 11S, and 7S) formed straight semi-flexible PNFs. Some differences in the capacity to form PNFs were observed between the two globulin fractions, with the smaller 7S protein being superior to 11S. The fibrillated protein from fava bean, 11S, and 7S generated more voluminous and more stable foams at 10 mg/mL than the corresponding non-fibrillated protein. However, this ability for fibrillated proteins to improve the foam properties seemed to be concentration-dependent, as at 1 mg/mL, the foams were less stable than those made from the non-fibrillated protein.

Place, publisher, year, edition, pages
MDPI AG, 2023
Keywords
plant protein, fava bean, amyloids, legumin, vicilin, 11S, 7S, microscopy, rheology
National Category
Nutrition and Dietetics
Identifiers
urn:nbn:se:kth:diva-324889 (URN)10.3390/foods12030521 (DOI)000930909100001 ()36766050 (PubMedID)2-s2.0-85147803394 (Scopus ID)
Note

QC 20230320

Available from: 2023-03-20 Created: 2023-03-20 Last updated: 2025-02-11Bibliographically approved
Herneke, A., Karkehabadi, S., Lu, J., Lendel, C. & Langton, M. (2023). Protein nanofibrils from mung bean: The effect of pH on morphology and the ability to form and stabilise foams. Food Hydrocolloids, 136, Article ID 108315.
Open this publication in new window or tab >>Protein nanofibrils from mung bean: The effect of pH on morphology and the ability to form and stabilise foams
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2023 (English)In: Food Hydrocolloids, ISSN 0268-005X, E-ISSN 1873-7137, Vol. 136, article id 108315Article in journal (Refereed) Published
Abstract [en]

Protein nanofibrils (PNFs) have potential food uses due to their favorable mechanical and rheological properties. In order to use plant-based protein nanofibrils (PNFs) in new sustainable food applications, a better under-standing is needed of the impact of pH on PNFs and their functional properties. In this study, we developed an improved method for generating PNFs from mung bean protein isolate and its globular 8S fraction. We then investigated how these PNFs are affected by increased pH and how pH affects their ability to form stable foams. PNFs were generated in acidic conditions (pH 2) by heating at 85 degrees C for 2-48 h. Formation of PNFs and the effect of increased pH on their stability were evaluated using thioflavin T fluorescence, electrophoretic gel separation, circular dichroism spectroscopy, atomic force microscopy and viscosity profiling. Foams were made by intense mixing with a homogeniser and evaluated for foam capacity, foam stability and bubble size distribution, using confocal imaging. The results showed that it is possible to optimise the fibrillation conditions for mung bean by generating a more pure initial protein isolate by salt extraction. The results also showed that pH alters the structure of PNFs by degradation and aggregation around the isoelectric point of the protein isolate. At neutral pH, the PNFs were slightly shorter than at the starting pH, but no longer formed aggregates. Fibrillated mung bean protein at pH 4-8 was found to have good foaming properties compared with non-fibrillated protein at the same conditions. The new knowledge generated in this study about how pH alters the structure and foaming properties of PNFs can pave the way for use of PNFs in new innovative food applications.

Place, publisher, year, edition, pages
Elsevier BV, 2023
Keywords
Plant protein, Foam capacity, Foam stability, Vicilin, 8S, Amyloid
National Category
Circular Food Process Technologies Food Biotechnology
Identifiers
urn:nbn:se:kth:diva-323759 (URN)10.1016/j.foodhyd.2022.108315 (DOI)000913247900001 ()2-s2.0-85141953524 (Scopus ID)
Note

QC 20230215

Available from: 2023-02-15 Created: 2023-02-15 Last updated: 2025-02-20Bibliographically approved
De Oliveira, D. H., Gowda, V., Sparrman, T., Riekel, C., Barth, A., Lendel, C. & Hedhammar, M. (2023). Structural studies of the C-terminal domain of Major ampullate Spidroin 1 present alpha-helical to coil/beta-sheet transition upon fiber formation. Paper presented at 37th Annual Meeting of The-Protein-Society (TPS), JUL 13-16, 2023, Boston, MA. Protein Science, 32(12)
Open this publication in new window or tab >>Structural studies of the C-terminal domain of Major ampullate Spidroin 1 present alpha-helical to coil/beta-sheet transition upon fiber formation
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2023 (English)In: Protein Science, ISSN 0961-8368, E-ISSN 1469-896X, Vol. 32, no 12Article in journal, Meeting abstract (Other academic) Published
Place, publisher, year, edition, pages
WILEY, 2023
National Category
Biochemistry Molecular Biology
Identifiers
urn:nbn:se:kth:diva-342742 (URN)001126426300334 ()
Conference
37th Annual Meeting of The-Protein-Society (TPS), JUL 13-16, 2023, Boston, MA
Note

QC 20240205

Available from: 2024-02-05 Created: 2024-02-05 Last updated: 2025-02-20Bibliographically approved
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0001-9238-7246

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