Identification and Application of Polymer‐Binding Peptides

Nanotopography-Induced Structural Anisotropy and Sarcomere Development in Human Cardiomyocytes Derived from Induced Pluripotent Stem Cells

“…PUA-binding peptide domains were screened from a rationally selected set of 15 peptide candidates that were previously reported to bind to polymeric materials. − In the screening assay, biotinylated PUABP candidates were allowed to self-assemble on nonpatterned PUA substrates where they interacted with streptavidin-Alexa conjugates to produce a fluorescent signal, and the intensity of this signal was quantified to determine the amount of peptide bound to the substrate (Figure A). From surface binding assays, five of the tested peptides produced a quantifiable fluorescence signal ( n = 4, Figure B).…”

“…Over the past decade, solid binding peptides have been utilized increasingly as biomolecular surface functionalization agents due to their selectivity and high affinity to the materials. These peptides have demonstrated specific and versatile biomolecular recognition-based self-assembly on a variety of inorganic materials such as metals, metal oxides, ceramics, − as well as on polymeric materials. − The biological nature of these short peptide sequences allows for the incorporation of additional functionalities, thereby providing a means for chimeric protein or peptide design. , The combination of the complex functionalities presented in one chimeric peptidic molecule enables adaptable surface functionalization by facilitating the formation of biomimetic interfaces where bioactive domains can be displayed with the desired orientation while building upon the self-assembly of the surface recognition domain. The self-organization of such biomolecular assemblies on surfaces of varying compositions and topographical complexities under physiological conditions make them highly desirable by eliminating the need for complex chemical reactions and harsh chemicals used in conventional chemical cross-linking systems.…”