ADP晶体{100}面族二维成核生长微观形貌的AFM研究

ADP晶体{100}面族微观形貌的非实时AFM(atomic force microscopy,AFM)成像表明,过饱和度σ=0.053时,晶面上出现二维成核生长;随σ增加至0.11,二维岛数量急剧增加,尺寸减小,分布渐趋均匀,二维成核生长逐渐增强,界面呈现出由光滑向粗糙转变的特征;各二维岛形状趋近于长条形,表现出各向异性,长轴平行于[001]晶向;二维岛上有单分子高度的台阶和台阶聚并后高度为2～3nm的大台阶;二维岛间融合时取向相同;σ=0.053时,融合后所形成的较大二维岛的生长呈现出周边快中心慢的情况,将可能导致产生晶体缺陷.     

KDP晶体相变界面微观形貌及大台阶形成的AFM观察

采用原子力显微镜实时和非实时观察了不同过饱和度下KDP晶体(100)面相变界面微观形貌,观察到晶体从生长死区恢复生长的过程;首次得到大台阶形成过程的实时AFM图像,解释了大台阶的形成机理;分析了台阶失稳的原因。结果表明,不同实验条件下,KDP(100)面相变界面均呈现为台阶面。在低过饱和度下,生长台阶来源于螺位错;在较高过饱和度下,层状台阶列来源于二维核。     

pH值对ADP晶体(100)面生长的影响

通过对40℃、不同pH值和过饱和度下ADP晶体(100)面法向生长速度的研究,发现在同一过饱和度下,改变pH值后晶面的生长速度明显加快。实验数据显示,在过饱和度较低时,(100)面的生长以螺旋位错生长机制为主;过饱和度较高时,以二维成核生长机制为主,而且pH值的改变会促使ADP晶体在较低的过饱和度下就从位错生长机制向二维成核生长机制转变。利用实验数据计算出了不同pH值下、二维成核生长机制控制晶体生长时的台阶棱边能。最后,运用原子力显微镜(AFM)非实时观察了不同过饱和度、不同pH值下生长的ADP晶体(100)面的微观形貌,发现与正常pH值相比,在较低的过饱和度下,pH=2.5和5.0的晶面上就出现了二维核。     

ZTS晶体(100)面生长过程的实时AFM研究

利用原子力显微镜(AFM)对不同生长条件下ZTS晶体(100)面生长过程进行实时观测发现,(100)面均呈现为台阶面,台阶分单台阶、聚并台阶和准聚并台阶3种。位错、缺陷和二维成核均可形成单台阶;聚并台阶以整体推移的方式生长,而准聚并台阶内的单台阶保持单台阶推移的特点。单台阶的推移展现出明显的各向异性。聚并台阶的聚并程度随着过饱和度增大而增大;台阶簇内台阶合并和不同生长源生成的沿不同推移方向推移的台阶相互影响引起台阶运动失稳均能导致聚并台阶的形成;聚并台阶列同步向前推移体现出生长的稳定性,随着生长进行,生长台阶各个位置的过饱和度差异会导致稳定性遭到破坏。另外发现,晶体表面存在优先成核位置,优先成核位置位于台阶边缘,且成核过程遵循成核—扩展—再次成核的规律性。     

硫脲硫酸锌晶体（100）面台阶生长动力学实时研究

运用光学显微镜实时观测了硫脲硫酸锌晶体（100）面台阶推移过程。获得了不同过饱和度、不同台阶高度、不同生长时间、不同台阶边缘扭折密度下的台阶推移速率;应用＂净流量＂模型解释了不同台阶推移速率的差异与过饱和度之间的依赖关系,计算了生长单元与台阶融合活化能及单台阶的动力学系数。通过分析发现台阶推移速率随过饱和度增加而线性增加,随台阶高度增加而下降;同一台阶推移速率随时间变化的现象与台阶重组过程有关;而台阶边缘扭折密度则从根本上决定了台阶推移速率的大小和变化趋势。     

棱角对NH4H2PO4晶体Z切片薄表面层生长影响的研究

本研究制备了具有不同形式棱角的NH₄H₂PO₄(ADP)晶体Z切片样品。通过实验, 观察不同Z切片薄表面层形成及生长特性, 并计算了不同棱角情况下薄表面层的切向生长速度V及其动力学系数β。结果表明, 正常棱角的缺失, 影响Z切片对其原有形态的“判断”, 进而影响薄表面层的形成及生长; 薄表面层在正常棱角处相遇形成相交角后, 将主要在相交角处形成并向棱边扩展生长, 表明棱角可能为薄表面层的主要生长源。此外, 计算结果显示, 正常棱角处薄表面层切向生长的平均生长动力学系数β_n为131.8 μm/s, 远大于棱角缺失后薄表面层切向生长的平均生长动力学系数β_a=11.6 μm/s, 即正常棱角缺失后, 薄表面层的切向生长速度将大大降低。     

ZTS晶体(100)面台阶聚并现象的AFM非实时研究

通过对301 K时,不同过饱和度以及掺杂2.5%(摩尔分数)尿素(σ=0.09)条件下生长的ZTS晶体进行AFM非实时扫描,对其(100)面的基本台阶以及聚并形成宏观台阶的形貌情况进行了研究。发现ZTS晶体(100)面在低过饱和度下(σ=0.03),以基本台阶推移为主,台阶高度约为0.553nm,近似为晶格参数a值的一半;在高过饱和度下(σ=0.09),以台阶聚并后的宏观台阶推移为主。而在同样的过饱和度下掺入尿素则会加剧台阶聚并的程度,该实验结果很好地符合了杂质诱导产生非对称台阶动力学系数理论模型。     

凝胶法制备Ba铁氧体的微观形态及磁性能

用溶胶-凝胶技术制备六角晶系BaFe12O19铁氧体超微粉末,采用热分析技术和XRD技术分析了其形成规律,运用扫描探针显微镜分析其微观形态,并测定了常温磁性能。结果表明：BaFe2O4和BaFe12O19的转变温度分别为414．55℃、755．78℃;800℃处理后得到的BaFe12O19超微粉末呈三种不同的形态,分别为圆形、带孔洞的圆形和圆环形;平均粒径为450nm左右;其厚度小于其直径;1000℃处理后的样品完全是BaFe12O19结构,其ds小于粗晶BaFe12O19铁氧体,而Hc大于粗晶肪BaFe12O19铁氧体。     

氧化锌纳米晶体的生长及生长机理分析

采用沉淀法生长了不同粒径且性能良好的氧化锌纳米晶体,探讨了晶粒尺寸与煅烧温度的变化关系,研究了ZnO纳米晶体的生长机理.通过实验验证了在中间产物Zn(OH)2中加入NH4HCO3后,ZnO纳米晶体实现了局域生长,很好地阻碍了晶核的过度生长,从而使生成的ZnO纳米晶体保持很小的粒径.煅烧温度较低时,ZnO纳米晶体的生长模式为正常扩散生长,煅烧温度在800℃时,发生了竞争生长现象.     

Direct evidence of lipid rafts by in situ atomic force microscopy

Lipid rafts are membrane microdomains enriched with cholesterol, glycosphingolipids, and proteins. Although they are broadly presumed to play a pivotal role in various cellular functions, there are still fierce debates about the composition, functions, and even existence of lipid rafts. Here high-resolution and time-lapse in situ atomic force microscopy is used to directly confirm the existence of lipid rafts in native erythrocyte membranes. The results indicate some important aspects of lipid rafts: most of the lipid rafts are in the size range of 100-300 nm and have irregular shape; the detergent-resistant membranes consist of cholesterol microdomains and are not likely the same as the lipid rafts; cholesterol contributes significantly to the formation and stability of the protein domains; and Band III is an important protein of lipid rafts in the inner leaflet of erythrocyte membranes, indicating that lipid rafts are exactly the functional domains in plasma membrane. This work provides direct evidence of the presence, size, and main constitutive protein of lipid rafts at a resolution of a few nanometers, which will pave the way for studying their structure and functions in detail.     

In situ tensile testing of nanofibers by combining atomic force microscopy and scanning electron microscopy

A nanomechanical testing set-up is developed by integrating an atomic force microscope (AFM) for force measurements with a scanning electron microscope (SEM) to provide imaging capabilities. Electrospun nanofibers of polyvinyl alcohol (PVA), nylon-6 and biological mineralized collagen fibrils (MCFs) from antler bone were manipulated and tensile-tested using the AFM-SEM set-up. The complete stress-strain behavior to failure of individual nanofibers was recorded and a diversity of mechanical properties observed, highlighting how this technique is able to elucidate mechanical behavior due to structural composition at nanometer length scales.     

In situ single-molecule detection of antibody-antigen binding by tapping-mode atomic force microscopy

We performed in situ detection of specific and nonspecific binding during immunoreaction on surfaces at the same location before and after analyte was injected using tapping-mode atomic force microscopy (TM-AFM) in liquid and demonstrated the ability of TM-AFM to monitor the occurrence of single-molecule binding events and to distinguish nonspecific from specific binding by examining topographical change. Two antigen/antibody pairs were investigated: chorionic gonadotropin (hCG)/mouse monoclonal anti-hCG and goat IgG (anti-intact hCG)/ mouse monoclonal anti-goat IgG. Antibody (or antigen) molecules were covalently immobilized on uniform mixed self-assembled monolayers (SAMs) terminated with carboxylic acid and hydroxyl groups. Mixed SAMs allow the control of the density of immobilized antibody (or antigen) on surfaces to achieve the detection of individual antigens, antibodies, and antigen/antibody complexes. This in situ TM-AFM-based detection method allows the single-molecule detection of antigen/antibody binding under near-physiological environment and the distinction of nonspecific from specific binding. It could be extended into a microarray.     

Growth processes of poly methylmethacrylate particles investigated by atomic force microscopy

The growth processes of poly methylmethacrylate (PMMA) particles prepared by soap-free emulsion polymerization at a reaction temperature 70°C are observed using scanning electron microscopy and atomic force microscopy to clarify the growth mechanisms at the molecular scale. Here, the use of a cationic initiator, V-50, enables us to synthesize positively charged PMMA, which then adsorbs electrostatically on the negatively charged mica plate with molecular scale smoothness. As a result, the following results are found. If the monomer concentration is high, PMMA particle size increases with increasing initiator concentration, otherwise particle size decreases with increasing initiator concentration. In the former case, the growth mechanism is very similar to that of the polystyrene particles we proposed; in the latter case, the phenomenon is thought to follow the LaMer diagram.     

Young’s modulus measurements of nanohoneycomb structures by flexural testing in atomic force microscopy

This paper determines the Young’s modulus of nanohoneycomb structures by flexural testing in an atomic force microscope (AFM). Since the cross-sectional area of nanohoneycomb structures varies along the structure, the area moment of inertia is not a constant. The area moment of inertia is also influenced by the porosity of the nanohoneycomb structure. An anodic aluminum oxide (AAO) film is fabricated as a nanohoneycomb structure. Young’s modulus of the AAO film, measured from the results of flexural testing in AFM, is in good agreement with the results of tensile tests in a Nano-UTM (universal testing machine).     

Nucleation and growth of elastin-like peptide fibril multilayers: an in situ atomic force microscopy study

Controlling how molecules assemble into complex supramolecular architectures requires careful consideration of the subtle inter-?and intra-molecular interactions that control their association. This is particularly crucial in the context of assembly at interfaces, where both surface chemistry and structure can play a role in directing structure formation. We report here the results of a study into the self-assembly of the elastin-like peptide EP I on structurally modified highly ordered pyrolytic graphite, including the role of spatial confinement on fibril nucleation and the growth of oriented fibril multilayers. In situ atomic force microscopy performed in fluid and at elevated temperature provided direct evidence of frustrated fibril nuclei and oriented growth of independent fibril domains. These results portend the application of this in situ strategy for studies of the nucleation and growth mechanisms of other fibril-?and amyloid-forming proteins.     

In situ observation of fluoride-ion-induced hydroxyapatite-collagen detachment on bone fracture surfaces by atomic force microscopy

The topography of freshly fractured bovine and human bone surfaces was determined by the use of atomic force microscopy (AFM). Fracture surfaces from both kinds of samples exhibited complex landscapes formed by hydroxyapatite mineral platelets with lateral dimensions ranging from ～90?nm × 60?nm to ～20?nm × 20?nm. Novel AFM techniques were used to study these fracture surfaces during various chemical treatments. Significant topographical changes were observed following exposure to aqueous solutions of ethylenediaminetetraacetic acid (EDTA) or highly concentrated sodium fluoride (NaF). Both treatments resulted in the apparent loss of the hydroxyapatite mineral platelets on a timescale of a few seconds. Collagen fibrils situated beneath the overlying mineral platelets were clearly exposed and could be resolved with high spatial resolution in the acquired AFM images. Time-dependent mass loss experiments revealed that the applied agents (NaF or EDTA) had very different resulting effects. Despite the fact that the two treatments exhibited nearly identical results following examination by AFM, bulk bone samples treated with EDTA exhibited a ～70% mass loss after 72?h, whereas for the NaF-treated samples, the mass loss was only of the order of ～10%. These results support those obtained from previous mechanical testing experiments, suggesting that enhanced formation of superficial fluoroapatite dramatically weakens the protein-hydroxyapatite interfaces. Additionally, we discovered that treatment with aqueous solutions of NaF resulted in the effective extraction of noncollagenous proteins from bone powder.