Proteins are one of the major classes of biomolecules that execute biological functions for maintenance of life.Various kinds of nanostructures self-assembled from proteins have been created in nature over millions of...Proteins are one of the major classes of biomolecules that execute biological functions for maintenance of life.Various kinds of nanostructures self-assembled from proteins have been created in nature over millions of years of evolution,including protein nanowires,layers and nanocages.These protein nanostructures can be reconstructed and equipped with desired new functions.Learning from and manipulating the self-assembly of protein nanostructures not only help to deepen our understanding of the nature of life but also offer new routes to fabricate novel nanomaterials for diverse applications.This review summarizes the recent research progress in this field,focusing on the characteristics,functionalization strategies,and applications of protein nanostructures.展开更多
Proteins play a vital role in different biological processes by forming complexes through precise folding with exclusive inter-and intra-molecular interactions.Understanding the structural and regulatory mechanisms un...Proteins play a vital role in different biological processes by forming complexes through precise folding with exclusive inter-and intra-molecular interactions.Understanding the structural and regulatory mechanisms underlying protein complex formation provides insights into biophysical processes.Furthermore,the principle of protein assembly gives guidelines for new biomimetic materials with potential appli-cations in medicine,energy,and nanotechnology.Atomic force microscopy(AFM)is a powerful tool for investigating protein assembly and interactions across spatial scales(single molecules to cells)and temporal scales(milliseconds to days).It has significantly contributed to understanding nanoscale architectures,inter-and intra-molecular interactions,and regulatory elements that determine protein structures,assemblies,and functions.This review describes recent advancements in elucidating protein assemblies with in situ AFM.We discuss the structures,diffusions,interac-tions,and assembly dynamics of proteins captured by conventional and high-speed AFM in near-native environments and recent AFM developments in the multimodal high-resolution imaging,bimodal imaging,live cell imaging,and machine-learning-enhanced data analysis.These approaches show the significance of broadening the horizons of AFM and enable unprecedented explorations of protein assembly for biomaterial design and biomedical research.展开更多
Protein adsorption onto polymer surfaces is a very complex and ubiquitous phenomenon whose integrated process impacts essential applications in our daily lives such as food packaging materials,health devices,diagnosti...Protein adsorption onto polymer surfaces is a very complex and ubiquitous phenomenon whose integrated process impacts essential applications in our daily lives such as food packaging materials,health devices,diagnostic tools,and medical products.Increasingly,novel polymer materials with greater chemical intricacy and reduced dimensionality are used for various applications involving adsorbed proteins on their surfaces.Hence,the nature of protein-surface interactions to consider is becoming much more complicated than before.A large body of literature exists for protein adsorption.However,most of these investigations have focused on collectively measured,ensemble-averaged protein behaviors that occur on macroscale and chemically unvarying polymer surfaces instead of direct measurements at the single protein or sub-protein level.In addition,interrogations of protein-polymer adsorption boundaries in these studies were typically carried out by indirect methods,whose insights may not be suitably applied for explaining individual protein adsorption processes occurring onto nanostructured,chemically varying polymer surfaces.Therefore,an important gap in our knowledge still exists that needs to be systematically addressed via direct measurement means at the single protein and sub-protein level.Such efforts will require multifaceted experimental and theoretical approaches that can probe multilength scales of protein adsorption,while encompassing both single proteins and their collective ensemble behaviors at the length scale spanning from the nanoscopic all the way to the macroscopic scale.In this review,key research achievements in nanoscale protein adsorption to date will be summarized.Specifically,protein adsorption studies involving polymer surfaces with their defining feature dimensions and associated chemical partitions comparable to the size of individual proteins will be discussed in detail.In this regard,recent works bridging the crucial knowledge gap in protein adsorption will be highlighted.New findings of intri展开更多
The intrinsic physical properties of the noble metal nanoparticles,which are highly sensitive to the nature of their local molecular environment,make such systems ideal for the detection of molecular recognition event...The intrinsic physical properties of the noble metal nanoparticles,which are highly sensitive to the nature of their local molecular environment,make such systems ideal for the detection of molecular recognition events.The current review describes the state of the art concerning molecular recognition of Noble metal nanoparticles.In the first part the preparation of such nanoparticles is discussed along with methods of capping and stabilization.A brief discussion of the three common methods of functionalization:Electrostatic adsorption;Chemisorption;Affinity-based coordination is given.In the second section a discussion of the optical and electrical properties of nanoparticles is given to aid the reader in understanding the use of such properties in molecular recognition.In the main section the various types of capping agents for molecular recognition;nucleic acid coatings,protein coatings and molecules from the family of supramolecular chemistry are described along with their numerous applications.Emphasis for the nucleic acids is on complementary oligonucleotide and aptamer recognition.For the proteins the recognition properties of antibodies form the core of the section.With respect to the supramolecular systems the cyclodextrins,calix[n]arenes,dendrimers,crown ethers and the cucurbitales are treated in depth.Finally a short section deals with the possible toxicity of the nanoparticles,a concern in public health.展开更多
基金supported by the National Natural Science Foundation of China(21890743,31771103,and 91527302)the National Key Research and Development Program of China(2017YFA0205503)+3 种基金the Strategic Priority Research Program of the Chinese Academy of Sciences(CAS)(XDB29050100)CAS Emergency Project of ASF Research(KJZD-SWL06 and KJZD-SWL07)Youth Innovation Promotion Association of CAS(2014308)Wuhan Huanghe Talents Program of Science and Technology。
文摘Proteins are one of the major classes of biomolecules that execute biological functions for maintenance of life.Various kinds of nanostructures self-assembled from proteins have been created in nature over millions of years of evolution,including protein nanowires,layers and nanocages.These protein nanostructures can be reconstructed and equipped with desired new functions.Learning from and manipulating the self-assembly of protein nanostructures not only help to deepen our understanding of the nature of life but also offer new routes to fabricate novel nanomaterials for diverse applications.This review summarizes the recent research progress in this field,focusing on the characteristics,functionalization strategies,and applications of protein nanostructures.
基金National Natural Science Foundation of China,Grant/Award Numbers:32371525,T2221001,92353304,T2350011Strategic Priority Research Program of the Chinese Academy of Sciences,Grant/Award Number:XDB37020105+5 种基金U.S.Department of EnergyOffice of ScienceOffice of Basic Energy Sciences,Grant/Award Number:FWP 65357Pacific Northwest National LaboratoryEnergy Frontier Research CentersCenter for the Science of Synthesis Across Scales,Grant/Award Number:DE-SC0019288。
文摘Proteins play a vital role in different biological processes by forming complexes through precise folding with exclusive inter-and intra-molecular interactions.Understanding the structural and regulatory mechanisms underlying protein complex formation provides insights into biophysical processes.Furthermore,the principle of protein assembly gives guidelines for new biomimetic materials with potential appli-cations in medicine,energy,and nanotechnology.Atomic force microscopy(AFM)is a powerful tool for investigating protein assembly and interactions across spatial scales(single molecules to cells)and temporal scales(milliseconds to days).It has significantly contributed to understanding nanoscale architectures,inter-and intra-molecular interactions,and regulatory elements that determine protein structures,assemblies,and functions.This review describes recent advancements in elucidating protein assemblies with in situ AFM.We discuss the structures,diffusions,interac-tions,and assembly dynamics of proteins captured by conventional and high-speed AFM in near-native environments and recent AFM developments in the multimodal high-resolution imaging,bimodal imaging,live cell imaging,and machine-learning-enhanced data analysis.These approaches show the significance of broadening the horizons of AFM and enable unprecedented explorations of protein assembly for biomaterial design and biomedical research.
基金D.H.C.,T.X,and J.T.acknowledge financial support on this work by the National Science Foundation(NSF Award Nos.CHE1404658,CHE1903857)from the Macromolecular,Supramolecular and Nanochemistry Program under the Division of Chemistry.J.H.acknowledges the NSF support from the Independent Research/Development(IR/D)program while serving at the National Science Foundation.
文摘Protein adsorption onto polymer surfaces is a very complex and ubiquitous phenomenon whose integrated process impacts essential applications in our daily lives such as food packaging materials,health devices,diagnostic tools,and medical products.Increasingly,novel polymer materials with greater chemical intricacy and reduced dimensionality are used for various applications involving adsorbed proteins on their surfaces.Hence,the nature of protein-surface interactions to consider is becoming much more complicated than before.A large body of literature exists for protein adsorption.However,most of these investigations have focused on collectively measured,ensemble-averaged protein behaviors that occur on macroscale and chemically unvarying polymer surfaces instead of direct measurements at the single protein or sub-protein level.In addition,interrogations of protein-polymer adsorption boundaries in these studies were typically carried out by indirect methods,whose insights may not be suitably applied for explaining individual protein adsorption processes occurring onto nanostructured,chemically varying polymer surfaces.Therefore,an important gap in our knowledge still exists that needs to be systematically addressed via direct measurement means at the single protein and sub-protein level.Such efforts will require multifaceted experimental and theoretical approaches that can probe multilength scales of protein adsorption,while encompassing both single proteins and their collective ensemble behaviors at the length scale spanning from the nanoscopic all the way to the macroscopic scale.In this review,key research achievements in nanoscale protein adsorption to date will be summarized.Specifically,protein adsorption studies involving polymer surfaces with their defining feature dimensions and associated chemical partitions comparable to the size of individual proteins will be discussed in detail.In this regard,recent works bridging the crucial knowledge gap in protein adsorption will be highlighted.New findings of intri
文摘The intrinsic physical properties of the noble metal nanoparticles,which are highly sensitive to the nature of their local molecular environment,make such systems ideal for the detection of molecular recognition events.The current review describes the state of the art concerning molecular recognition of Noble metal nanoparticles.In the first part the preparation of such nanoparticles is discussed along with methods of capping and stabilization.A brief discussion of the three common methods of functionalization:Electrostatic adsorption;Chemisorption;Affinity-based coordination is given.In the second section a discussion of the optical and electrical properties of nanoparticles is given to aid the reader in understanding the use of such properties in molecular recognition.In the main section the various types of capping agents for molecular recognition;nucleic acid coatings,protein coatings and molecules from the family of supramolecular chemistry are described along with their numerous applications.Emphasis for the nucleic acids is on complementary oligonucleotide and aptamer recognition.For the proteins the recognition properties of antibodies form the core of the section.With respect to the supramolecular systems the cyclodextrins,calix[n]arenes,dendrimers,crown ethers and the cucurbitales are treated in depth.Finally a short section deals with the possible toxicity of the nanoparticles,a concern in public health.
