Swirl-like nanospiral is a common structure found in free-swimming biological systems,such as microtubules and actin filaments or slender bacteria.It is desired for artificially designed dynamic nanomaterials.However,...Swirl-like nanospiral is a common structure found in free-swimming biological systems,such as microtubules and actin filaments or slender bacteria.It is desired for artificially designed dynamic nanomaterials.However,the spiral formation has rarely been reported in both engineered peptides and regenerated proteins.Herein,we report that such a unique assembly behavior can be achieved by using a fusion peptide consisting of a silk-derived peptide(i.e.,GAGAGAGY)and a hydrophobic,photoresponsive azobenzene(Azo)segment.In this fusion structure,GAGAGAGY acts as a domain that spontaneously forms an elongated filament in an aqueous solution,while Azo acts as a"light-operated switch"that can undergo photoinduced isomerization to modulate the self-propulsion forces and assembly behavior.With this design,the critical factors that affect the assembly of Azo-GAGAGAGY filament,including(i)length and flexibility of filaments;(ii)propulsion,and(iii)excluded volume interactions force the tip of the filament to wind up,can be regulated to realize the spiral formation.In addition,the configurations of Azo-GAGAGAGY filaments,such as straight nanoribbons,wavy nanoribbons,single-circle spiral,and multiple-circle spiral,can be facilely mediated by changing the preparation procedure,concentration,and pH value of Azo-GAGAGAGY solution,as these changes have significant influences on self-propulsion forces.Our findings can help in the better understanding of nonequilibrium thermodynamics and collective behavior of biological systems.The findings can be used as a guideline for the designs of nanoactuators,microswimmers,transformable microrobots,and intelligent drug carriers.展开更多
基金This work is supported by the National Natural Science Foundation of China(No.21935002).
文摘Swirl-like nanospiral is a common structure found in free-swimming biological systems,such as microtubules and actin filaments or slender bacteria.It is desired for artificially designed dynamic nanomaterials.However,the spiral formation has rarely been reported in both engineered peptides and regenerated proteins.Herein,we report that such a unique assembly behavior can be achieved by using a fusion peptide consisting of a silk-derived peptide(i.e.,GAGAGAGY)and a hydrophobic,photoresponsive azobenzene(Azo)segment.In this fusion structure,GAGAGAGY acts as a domain that spontaneously forms an elongated filament in an aqueous solution,while Azo acts as a"light-operated switch"that can undergo photoinduced isomerization to modulate the self-propulsion forces and assembly behavior.With this design,the critical factors that affect the assembly of Azo-GAGAGAGY filament,including(i)length and flexibility of filaments;(ii)propulsion,and(iii)excluded volume interactions force the tip of the filament to wind up,can be regulated to realize the spiral formation.In addition,the configurations of Azo-GAGAGAGY filaments,such as straight nanoribbons,wavy nanoribbons,single-circle spiral,and multiple-circle spiral,can be facilely mediated by changing the preparation procedure,concentration,and pH value of Azo-GAGAGAGY solution,as these changes have significant influences on self-propulsion forces.Our findings can help in the better understanding of nonequilibrium thermodynamics and collective behavior of biological systems.The findings can be used as a guideline for the designs of nanoactuators,microswimmers,transformable microrobots,and intelligent drug carriers.
