期刊
NANOMATERIALS
卷 13, 期 19, 页码 -出版社
MDPI
DOI: 10.3390/nano13192645
关键词
helical barrel; amphiphilic peptide; higher order assembly; biomaterial; 3D matrix; cargo
In this study, disulfide-stapled helical barrels containing ligands for metal ions were synthesized, which, through metal-ion-promoted assembly, generated higher order assemblies with hydrophobic cavities. These peptide-based biomaterials have potential for various biotechnology applications.
Peptide-based helical barrels are a noteworthy building block for hierarchical assembly, with a hydrophobic cavity that can serve as a host for cargo. In this study, disulfide-stapled helical barrels were synthesized containing ligands for metal ions on the hydrophilic face of each amphiphilic peptide helix. The major product of the disulfide-stapling reaction was found to be composed of five amphiphilic peptides, thereby going from a 16-amino-acid peptide to a stapled 80-residue protein in one step. The structure of this pentamer, 5HB1, was optimized in silico, indicating a significant hydrophobic cavity of similar to 6 angstrom within a helical barrel. Metal-ion-promoted assembly of the helical barrel building blocks generated higher order assemblies with a three-dimensional (3D) matrix morphology. The matrix was decorated with hydrophobic dyes and His-tagged proteins both before and after assembly, taking advantage of the hydrophobic pocket within the helical barrels and coordination sites within the metal ion-peptide framework. As such, this peptide-based biomaterial has potential for a number of biotechnology applications, including supplying small molecule and protein growth factors during cell and tissue growth within the matrix.
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