Amyloid Formation of Stefin B Protein Studied by Infrared Spectroscopy.

Novak, Urban; Žerovnik, Eva; Taler-Verčič, Ajda; Žnidarič, MagdaTušek; Zupančič, Barbara; Grdadolnik, Jože (2023). Amyloid Formation of Stefin B Protein Studied by Infrared Spectroscopy. Frontiers in bioscience (Landmark edition), 28(3), p. 46. IMR Press 10.31083/j.fbl2803046

[img]
Preview
Text
37005760.pdf - Published Version
Available under License Creative Commons: Attribution (CC-BY).

Download (4MB) | Preview

BACKGROUND

Stefin B, an established model protein for studying the stability and mechanism of protein folding, was used for monitoring protein aggregation and formation of amyloid structure by infrared spectroscopy.

METHODS

The analyses of the integral intensities of the low frequency part of the Amide I band, which is directly connected to the appearance of the cross-β structure reveals the temperature but not pH dependence of stefin B structure.

RESULTS

We show that pH value has significant role in the monomer stability of stefin B. Protein is less stable in acidic environment and becomes more stable in neutral or basic conditions. While in the case of the Amide I band area analysis we apply only spectral regions characteristic for only part of the protein in cross-β structure, the temperature study using multivariate curve resolution (MCR) analysis contains also information about the protein conformation states which do not correspond to native protein nor protein in cross-β structure.

CONCLUSIONS

These facts results in the slightly different shapes of fitted sigmoid functions fitted to the weighted amount of the second basic spectrum (sc2), which is the closed approximation of the protein spectra with cross-β structure. Nevertheless, the applied method detects the initial change of the protein structure. Upon the analysis of infrared data a model for stefin B aggregation is proposed.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Department of Haematology, Oncology, Infectious Diseases, Laboratory Medicine and Hospital Pharmacy (DOLS) > Clinic of Medical Oncology

UniBE Contributor:

Novak, Urban

Subjects:

600 Technology > 610 Medicine & health

ISSN:

2768-6698

Publisher:

IMR Press

Language:

English

Submitter:

Teuta Bytyqi

Date Deposited:

12 Dec 2023 13:58

Last Modified:

17 Dec 2023 02:32

Publisher DOI:

10.31083/j.fbl2803046

PubMed ID:

37005760

Uncontrolled Keywords:

aggregation amyloid formation infrared spectroscopy stefin B structure analysis

BORIS DOI:

10.48350/190067

URI:

https://boris.unibe.ch/id/eprint/190067

Actions (login required)

Edit item Edit item
Provide Feedback