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Sökning: WFRF:(Kjellström Sven) > (2015-2019) > Adsorption of unfol...
- Khan, AshharLund University,Lunds universitet,Biofysikalisk kemi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biophysical Chemistry,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,Indian Institute of Technology (författare)
Adsorption of unfolded Cu/Zn superoxide dismutase onto hydrophobic surfaces catalyzes its formation of amyloid fibrils
- Artikel/kapitelEngelska2019
Förlag, utgivningsår, omfång ...
- 2019-09-06
- Oxford University Press (OUP),2019
- electronicrdacarrier
Nummerbeteckningar
- LIBRIS-ID:oai:lup.lub.lu.se:790e852b-bafd-494d-be62-caa6a8013aab
- https://lup.lub.lu.se/record/790e852b-bafd-494d-be62-caa6a8013aabURI
- https://doi.org/10.1093/protein/gzz033DOI
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- Språk:engelska
- Sammanfattning på:engelska &svenska
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- Intracellular aggregates of superoxide dismutase 1 (SOD1) are associated with amyotrophic lateral sclerosis. In vivo, aggregation occurs in a complex and dense molecular environment with chemically heterogeneous surfaces. To investigate how SOD1 fibril formation is affected by surfaces, we used an in vitro model system enabling us to vary the molecular features of both SOD1 and the surfaces, as well as the surface area. We compared fibril formation in hydrophilic and hydrophobic sample wells, as a function of denaturant concentration and extraneous hydrophobic surface area. In the presence of hydrophobic surfaces, SOD1 unfolding promotes fibril nucleation. By contrast, in the presence of hydrophilic surfaces, increasing denaturant concentration retards the onset of fibril formation. We conclude that the mechanism of fibril formation depends on the surrounding surfaces and that the nucleating species might correspond to different conformational states of SOD1 depending on the nature of these surfaces.
- Intracellular aggregates of superoxide dismutase 1 (SOD1) are associated with amyotrophic lateral sclerosis. In vivo, aggregation occurs in a complex and dense molecular environment with chemically heterogeneous surfaces. To investigate how SOD1 fibril formation is affected by surfaces, we used an in vitro model system enabling us to vary the molecular features of both SOD1 and the surfaces, as well as the surface area. We compared fibril formation in hydrophilic and hydrophobic sample wells, as a function of denaturant concentration and extraneous hydrophobic surface area. In the presence of hydrophobic surfaces, SOD1 unfolding promotes fibril nucleation. By contrast, in the presence of hydrophilic surfaces, increasing denaturant concentration retards the onset of fibril formation. We conclude that the mechanism of fibril formation depends on the surrounding surfaces and that the nucleating species might correspond to different conformational states of SOD1 depending on the nature of these surfaces.
Ämnesord och genrebeteckningar
- NATURVETENSKAP Kemi Fysikalisk kemi hsv//swe
- NATURAL SCIENCES Chemical Sciences Physical Chemistry hsv//eng
- NATURVETENSKAP Biologi Biokemi och molekylärbiologi hsv//swe
- NATURAL SCIENCES Biological Sciences Biochemistry and Molecular Biology hsv//eng
- NATURVETENSKAP Biologi Strukturbiologi hsv//swe
- NATURAL SCIENCES Biological Sciences Structural Biology hsv//eng
Biuppslag (personer, institutioner, konferenser, titlar ...)
- Weininger, UlrichLund University,Lunds universitet,Biofysikalisk kemi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biophysical Chemistry,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)bpc-uiw (författare)
- Kjellström, SvenLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Masspektrometri,Sektion V,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,BioMS,Forskargrupper vid Lunds universitet,CEBMMS PI,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,Mass Spectrometry,Section V,Department of Clinical Sciences, Lund,Faculty of Medicine,Lund University Research Groups(Swepub:lu)bioc-skj (författare)
- Deep, ShashankIndian Institute of Technology (författare)
- Akke, MikaelLund University,Lunds universitet,Biofysikalisk kemi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biophysical Chemistry,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)fkm2-mak (författare)
- Biofysikalisk kemiCentrum för Molekylär Proteinvetenskap (creator_code:org_t)
Sammanhörande titlar
- Ingår i:Protein Engineering Design & Selection: Oxford University Press (OUP)32:2, s. 77-851741-01261741-0134
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