Publication | Open Access
Designing Sequence-Defined Peptoids for Biomimetic Control over Inorganic Crystallization
30
Citations
97
References
2021
Year
Supramolecular AssemblyEngineeringBiomimetic MaterialsPeptide EngineeringPeptide ScienceChemistryBiomimetic ChemistrySurfactant-like Soluble AdditivesCrystal FormationHybrid MaterialsBiopolymersInorganic CrystallizationMolecular ModelingBiomolecular EngineeringSelf-assemblyPeptoidBiotechnologySynthetic BiologyPeptide Synthesis
Crystallization defines what the world is all about, ranging from biomineralization in living organisms to various materials in our lives. During these processes, peptides and proteins involved in biomineralization set excellent examples of additive-controlled crystallization. To mimic these natural systems and develop biomimetic approaches for controlling inorganic crystallization, sequence-defined peptoids, as one of the most advanced synthetic foldamers that mimic peptides and proteins, have been recently designed and explored for directing the formation of inorganic (nano)materials acting as surfactant-like soluble additives or self-assembled scaffolds due to their unique advantages (e.g., high programmability and stability). In this review, we extract the main concepts of peptoid engineering and highlight the recent advances in peptoid-controlled inorganic crystal formation. Our focus is to correlate the peptoid side chain chemistry with the morphological and kinetic control over inorganic (nano)crystal formation and to understand the principles in these biomimetic inorganic crystallization systems with respect to the predictive synthesis of organic–inorganic hybrid materials with desirable structures and physicochemical properties.
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