Stimuli‐Responsive Natural Proteins and Their Applications

Abstract

Natural proteins are essential biomacromolecules that fulfill versatile functions in the living organism, such as their usage as cytoskeleton, nutriment transporter, homeostasis controller, catalyzer, or immune guarder. Due to the excellent mechanical properties and good biocompatibility/biodegradability, natural protein-based biomaterials are well equipped for prospective applications in various fields. Among these natural proteins, stimuli-responsive proteins can be reversibly and precisely manipulated on demand, rendering the protein-based biomate-rials promising candidates for numerous applications, including disease detection, drug delivery, bio-sensing, and regenerative medicine. Therefore, we present some typical natural proteins with diverse physical stimuli-responsive properties, including temperature, light, force, electrical, and magnetic sensing in this review. The structure-function mechanism of these proteins is discussed in detail. Finally, we give a summary and perspective for the development of stimuli-responsive proteins.

Towards predictive control of reversible nanoparticle assembly with solid-binding proteins

“…Together with prior insights, the experimental validation of the model's predictive power and the improved understanding of the sfGFP::Car9-Car9-SiNP system garnered in this study sets the stage for the expansion of the concept to charged nanoparticles beyond silica (e.g., common and complex metal oxides, nitrides and carbides) and solid-binding proteins beyond sfGFP::Car9-Car9, including those selected or designed for self-assembly 25 and responsiveness to orthogonal stimuli. 49 Unlike with traditional nanoparticle functionalization schemes, the goal will not be to maximize ligand coverage but rather to leave enough of the particle surface solvent-accessible so as to enable sufficient repulsive interactions to finely balance protein-SiNP interactions that are themselves dependent on the distance separating SBPs and their relative affinity for the particle surface. We finally note that the use of anisotropic particles, the introduction of additional constraints (e.g., steric interactions), 50,51 and the delicate coupling to translational and orientational particle dynamics, 15,52 should provide a rich playground for the fabrication of reconfigurable protein-based materials with applications in catalysis, opto-electronics, and biomedicine.…”

“…, common and complex metal oxides, nitrides and carbides) and solid-binding proteins beyond sfGFP::Car9–Car9, including those selected or designed for self-assembly 25 and responsiveness to orthogonal stimuli. 49 Unlike with traditional nanoparticle functionalization schemes, the goal will not be to maximize ligand coverage but rather to leave enough of the particle surface solvent-accessible so as to enable sufficient repulsive interactions to finely balance protein–SiNP interactions that are themselves dependent on the distance separating SBPs and their relative affinity for the particle surface. We finally note that the use of anisotropic particles, the introduction of additional constraints ( e.g.…”

Toward Data-Driven Many-Body Simulations of Biomolecules in Solution: N-Methyl Acetamide as a Proxy for the Protein Backbone

“…In these sequences, each amino acid is connected to its neighbors by peptide bonds . Proteins play key roles in nearly all biological processes taking place in living systems, from catalyzing metabolic reactions and replicating DNA to responding to stimuli and transporting molecules from one location to another …”

“…3 In these sequences, each amino acid is connected to its neighbors by peptide bonds. 4 Proteins play key roles in nearly all biological processes taking place in living systems, from catalyzing metabolic reactions 5 and replicating DNA 6 to responding to stimuli 7 and transporting molecules from one location to another. 8 The hydration properties of a protein can have a considerable impact on how the protein folds into a threedimensional shape and carries out its biological functions in solution.…”

Photoallosteric Polymersomes toward On‐Demand Drug Delivery and Multimodal Cancer Immunotherapy

“…[8,9,17,18] In nature, some proteins are responsive to exogenous light, magnetic fields, heat, and other physical stimuli. [19][20][21][22][23] For example, bacteriorhodopsin as a light-driven proton pump and a model membrane transport protein could change its conformation after photoactivation, resulting in unidirectional proton transport. [24] The light, oxygen, and voltage sensing domain 2 is a plant-derived photoreceptor protein of which α-helicity is reversibly lost upon light irradiation, leading to further cascade reactions.…”