Premium
Peptides that form β‐sheets on hydrophobic surfaces accelerate surface‐induced insulin amyloidal aggregation
Author(s) -
Nault Laurent,
Vendrely Charlotte,
Bréchet Yves,
Bruckert Franz,
Weidenhaupt Marianne
Publication year - 2013
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.2012.11.036
Subject(s) - peptide , insulin , chemistry , biophysics , hydrophobic effect , protein aggregation , sequence (biology) , peptide sequence , in vitro , biochemistry , biology , endocrinology , gene
Interactions between proteins and material or cellular surfaces are able to trigger protein aggregation in vitro and in vivo. The human insulin peptide segment LVEALYL is able to accelerate insulin aggregation in the presence of hydrophobic surfaces. We show that this peptide needs to be previously adsorbed on a hydrophobic surface to induce insulin aggregation. Moreover, the study of different mutant peptides proves that its sequence is less important than the secondary structure of the adsorbed peptide on the surface. Indeed, these pro‐aggregative peptides act by providing stable β‐sheets to incoming insulin molecules, thereby accelerating insulin adsorption locally and facilitating the conformational changes required for insulin aggregation. Conversely, a peptide known to form α‐helices on hydrophobic surfaces delays insulin aggregation.