Literature DB >> 25551549

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

Vladimir V Egorov1, Dmitry V Lebedev, Aram A Shaldzhyan, Alexey K Sirotkin, Andrey N Gorshkov, Olga A Mirgorodskaya, Natalia A Grudinina, Andrey V Vasin, Michael M Shavlovsky.   

Abstract

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.

Entities:  

Keywords:  Fibrillogenesis; GYDTQAIVENNESTEYG; conformation transmission; lactalbumin; short peptides; spontaneous hydrolysis

Mesh：

Substances：

Year:  2014        PMID： 25551549      PMCID： PMC4601391          DOI： 10.4161/19336896.2014.983745

Source DB:  PubMed          Journal:  Prion        ISSN： 1933-6896            Impact factor:   3.931


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10.  Atomic force microscopy study of peptides homologous to beta-domain of alpha-lactalbumins.

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  3 in total

Review 1.  α-Lactalbumin, Amazing Calcium-Binding Protein.

Authors:  Eugene A Permyakov
Journal:  Biomolecules       Date:  2020-08-20

Review 2.  Peptide-Induced Amyloid-Like Conformational Transitions in Proteins.

Authors:  Vladimir Egorov; Natalia Grudinina; Andrey Vasin; Dmitry Lebedev
Journal:  Int J Pept       Date:  2015-09-08

3.  Nicking and fragmentation are responsible for α-lactalbumin amyloid fibril formation at acidic pH and elevated temperature.

Authors:  Rajesh Mishra
Journal:  Protein Sci       Date:  2021-06-17       Impact factor: 6.993
  3 in total

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