Amyloidogenic peptide homologous to fragment 129–148 of human myocilin

2022

Preprint

Using a set of programs for analyzing the primary structure of amyloidogenic proteins, we analyzed the primary structure of the of the COVID-19 NSP7 protein. Peptides containing potential amyloidogenic determinants in the primary structure have been synthesized and shown to be capable of forming amyloid-like fibrils in vitro. In the future, this peptide can be used as a basis for creating antiviral agents that act directly on the spatial structure of the NSP7 subunit of the COVID-19 polymerase.

Section: Resultsmentioning

confidence: 99%

Peptide from NSP7 is able to form amyloid-like fibrils: artifact or challenge to drug design?

Garmay

Rubel

2022

Preprint

“…The role of repeats in fibrillogenesis has been shown for the prion protein PrP [ 20 ] and for alpha-synuclein [ 21 ]. The leucine zipper motif located within myocilin usually forms an alpha-helix structure but is also prone to fibrillogenesis even under normal physiological conditions [ 22 ]. It would appear that the presence of easily identifiable repetitive sequences in these proteins is evidence of their relatively recent evolutionary origin [ 23 ].…”

Section: The Role Of Primary Structure Motifs In Conformational Trmentioning

confidence: 99%

Peptide-Induced Amyloid-Like Conformational Transitions in Proteins

International Journal of Peptides

Грудинина

Васин

et al. 2015

Changes in protein conformation can occur both as part of normal protein functioning and during disease pathogenesis. The most common conformational diseases are amyloidoses. Sometimes the development of a number of diseases which are not traditionally related to amyloidoses is associated with amyloid-like conformational transitions of proteins. Also, amyloid-like aggregates take part in normal physiological processes such as memorization and cell signaling. Several primary structural features of a protein are involved in conformational transitions. Also the protein proteolytic fragments can cause the conformational transitions in the protein. Short peptides which could be produced during the protein life cycle or which are encoded by short open reading frames can affect the protein conformation and function.

“…Amyloid fibril formation is a common phenomenon in human pathology. 1 Recent studies have shown that certain diseases such as hereditary glaucoma 2,3 or influenza infection 4 include a stage of amyloid-like oligomerization and amyloid fibril formation. A universal strategy for amyloidosis treatment currently has still yet to be developed.…”

Section: Introductionmentioning

confidence: 99%

A conservative mutant of a proteolytic fragment produced during fibril formation enhances fibrillogenesis

Лебедев

Shaldzhyan

et al. 2014

Prion

The fibrillogenesis of a peptide corresponding to residues 35-51 of human α-lactalbumin (¹GYDTQAIVENNESTEYG¹⁷) can be dramatically enhanced by the addition of a tetrapeptide TDYG homologous to its C-terminus (TEYG). Generation of spontaneous hydrolytic products similar to this peptide was demonstrated by mass-spectrometry analysis of GYDTQAIVENNESTEYG peptide solution components during fibrillogenesis. Possible mechanisms and roles of short peptides in protein metabolism are discussed.