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Formation of supramolecular structures of a native‐like protein in the presence of amphiphilic peptides: Variations in aggregate morphology
Author(s) -
Artemova Natalya,
Stein-Margolina Vita,
Smirnova Ekaterina,
Gurvits Bella
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.12.017
Subject(s) - circular dichroism , amphiphile , chemistry , supramolecular chemistry , biophysics , dynamic light scattering , peptide , amyloid (mycology) , protein aggregation , native state , biochemistry , crystallography , nanotechnology , polymer , nanoparticle , organic chemistry , biology , materials science , copolymer , crystal structure , inorganic chemistry
A striking potential of the amphiphilic dipeptides, Arg‐Phe or Asp‐Phe, to induce aggregation of a model protein, alcohol dehydrogenase in its native‐like state, has been demonstrated under physiologically relevant conditions, using dynamic light scattering, fluorescence spectroscopy, circular dichroism, transmission electron‐ and atomic force microscopy. The peptide action resulted in accumulation of a variety of morphologically distinct supramolecular structures profoundly differing from those generated by the heat‐induced aggregation at the early stages of the process, when amyloid fibril assemblies were not detectable. The biogenic amphiphilic agents are suggested to act as regulators of structural transformations of native‐like proteins.