Next Article in Journal
Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis
Next Article in Special Issue
Solution of Levinthal’s Paradox and a Physical Theory of Protein Folding Times
Previous Article in Journal
The Role of Reactive Oxygen Species in Arsenic Toxicity
Previous Article in Special Issue
How Quickly Do Proteins Fold and Unfold, and What Structural Parameters Correlate with These Values?
Open AccessArticle

The Kinetics of Amyloid Fibril Formation by de Novo Protein Albebetin and Its Mutant Variants

1
Institute of Protein Research, Pushchino, Moscow 142290, Russia
2
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho–Maklaya st. 16/10, Moscow 117997, Russia
3
Faculty of Biology and Biotechnologies, National Research University Higher School of Economics, Moscow 117312, Russia
4
Biology Department, Lomonosov Moscow State University, Leninskie gory, 1/12, Moscow 119899, Russia
*
Authors to whom correspondence should be addressed.
Biomolecules 2020, 10(2), 241; https://doi.org/10.3390/biom10020241
Received: 29 November 2019 / Revised: 1 February 2020 / Accepted: 3 February 2020 / Published: 5 February 2020
Engineering of amyloid structures is one of the new perspective areas of protein engineering. Studying the process of amyloid formation can help find ways to manage it in the interests of medicine and biotechnology. One of the promising candidates for the structural basis of artificial functional amyloid fibrils is albebetin (ABB), an artificial protein engineered under the leadership of O.B. Ptitsyn. Various aspects of the amyloid formation of this protein and some methods for controlling this process are investigated in this paper. Four stages of amyloid fibrils formation by this protein from the first non-fibrillar aggregates to mature fibrils and large micron-sized complexes have been described in detail. Dependence of albebetin amyloids formation on external conditions and some mutations also have been described. The introduction of similar point mutations in the two structurally identical α-β-β motifs of ABB lead to different amiloidogenesis kinetics. The inhibitory effect of a disulfide bond and high pH on amyloid fibrils formation, that can be used to control this process, was shown. The results of this work are a good basis for the further design and use of ABB-based amyloid constructs.
Keywords: amyloidogenesis; amyloid fibrils; cross-beta structure; albebetin; de novo proteins amyloidogenesis; amyloid fibrils; cross-beta structure; albebetin; de novo proteins
MDPI and ACS Style

Balobanov, V.; Chertkova, R.; Egorova, A.; Dolgikh, D.; Bychkova, V.; Kirpichnikov, M. The Kinetics of Amyloid Fibril Formation by de Novo Protein Albebetin and Its Mutant Variants. Biomolecules 2020, 10, 241.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop