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Mussel‐Glue Inspired Adhesives: A Study on the Relevance of l ‐Dopa and the Function of the Sequence at Nanomaterial‐Peptide Interfaces
Author(s) -
Venkatareddy Narendra L.,
Wilke Patrick,
Ernst Natalia,
Horsch Justus,
Weber Marcus,
Dallmann Andre,
Börner Hans G.
Publication year - 2019
Publication title -
advanced materials interfaces
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.671
H-Index - 65
ISSN - 2196-7350
DOI - 10.1002/admi.201900501
Subject(s) - peptide , adhesive , materials science , glue , molecular dynamics , two dimensional nuclear magnetic resonance spectroscopy , nuclear overhauser effect , nanomaterials , mussel , protein structure , biophysics , crystallography , nanotechnology , stereochemistry , chemistry , nuclear magnetic resonance spectroscopy , biochemistry , biology , computational chemistry , composite material , ecology , layer (electronics)
Mussel glue‐proteins undergo structural transitions at material interfaces to optimize adhesive surface contacts. Those intriguing structure responses are mimicked by a mussel‐glue mimetic peptide (HSY*SGWSPY*RSG (Y* = l ‐Dopa)) that was previously selected by phage‐display to adhere to Al 2 O 3 after enzymatic activation. Molecular level insights into the full‐length adhesion domain at Al 2 O 3 surfaces are provided by a divergent‐convergent analysis, combining nuclear Overhauser enhancement based 2D NOESY and saturation transfer difference NMR analysis of submotifs along with molecular dynamics simulations of the full‐length peptide. The peptide is divided into two submotifs, each containing one Dopa “anchor” (Motif‐1 and 2). The analysis proves Motif‐1 to constitute a dynamic Al 2 O 3 binder and adopting an “M”‐structure with multiple surface contacts. Motif‐2 binds stronger by two surface contacts, forming a compact “C”‐structure. Taking these datasets as constraints enables to predict the structure and propose a binding process model of the full‐length peptide adhering to Al 2 O 3 .