Amyloid fibril formation from human and bovine serum albumin followed by quasi-simultaneous Fourier-transform infrared (FT-IR) spectroscopy and static light scattering (SLS)

Human and bovine serum albumins are widely known proteins that can form amyloid fibrils under destabilizing conditions. Use of well-known proteins with easily-controlled aggregation process, and comparison of these processes for similar proteins from different species, could help elucidate the natur...

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Bibliographic Details
Published inEuropean biophysics journal Vol. 41; no. 11; pp. 931 - 938
Main Authors de la Arada, Igor, Seiler, Christian, Mäntele, Werner
Format Journal Article
LanguageEnglish
Published Berlin/Heidelberg Springer-Verlag 01.11.2012
Springer Nature B.V
Subjects
Amyloid - chemistry
Animals
Biochemistry
Biological and Medical Physics
Biomedical and Life Sciences
Biophysics
Cattle
Cell Biology
Disease
Fourier transforms
Humans
Infrared spectroscopy
Life Sciences
Light
Light scattering
Membrane Biology
Nanotechnology
Neurobiology
Original Paper
Protein Folding
Protein Structure, Secondary
Proteins
Scattering, Radiation
Serum Albumin - chemistry
Serum Albumin, Bovine - chemistry
Spectroscopy, Fourier Transform Infrared
Spectrum analysis
Bovine serum albumin (BSA)
Amyloid
Human serum albumin (HSA)
Two-dimensional correlation spectroscopy (2DCOS)
Fourier-transform infrared (FT-IR) spectroscopy
Static light scattering (SLS)
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Summary:Human and bovine serum albumins are widely known proteins that can form amyloid fibrils under destabilizing conditions. Use of well-known proteins with easily-controlled aggregation process, and comparison of these processes for similar proteins from different species, could help elucidate the nature of the aggregation process implicated in many degenerative diseases, for example Alzheimer’s, Parkinson’s, or type II diabetes. In this work both amyloidogenic mechanisms have been studied by use of infrared spectroscopy in combination with static light scattering, enabling analysis of intra and intermolecular processes and measurement of prefibril and fibril growing quasi-simultaneously. Deeper insight into the rearrangements of the secondary structure of the proteins concomitant with the aggregation process has also been gained by mathematical analysis of the infrared spectra by two-dimensional correlation spectroscopy (2DCOS).
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ISSN:0175-7571
1432-1017
DOI:10.1007/s00249-012-0845-1