Asylum 1 mfp 3d afm system

Example 1

Atomic Force Microscopy (AFM) images of ST14 and T14 peptides were investigated to visualize their nano structures. Samples were prepared by placing an aliquot of approximately 50 microliters (μl) of the peptide (100 micromolar (μM)) solution on the surface (9 millimeters (mm) in diameter) of a mica surface. Each sample was left on the mica for about 30 seconds (s) and then rinsed with aliquots of 100 μl of Milli-Q (ultrapure) water to remove unattached peptides. The sample on the mica surface was then air-dried for AFM observation. AFM was performed with Asylum-1 MFP-3D AFM System (Asylum Research, Santa Barbara, Calif.) using a tapping mode. The images utilized an Olympus Si tip (AC240FS). The cantilever's free resonance frequency was 70 kHz. Height images were recorded with 256×256 pixels resolution.

As shown in FIGS. 3 and 4, AFM morphological studies demonstrated that ST14 forms self-assembled nanofibers. Aggregates have been detected in T14, as shown in FIGS. 5 and 6.

Example 1

Atomic Force Microscopy (AFM) images of ST14 and T14 peptides were investigated to visualize their nano structures. Samples were prepared by placing an aliquot of approximately 50 microliters (μl) of the peptide (100 micromolar (μM)) solution on the surface (9 millimeters (mm) in diameter) of a mica surface. Each sample was left on the mica for about 30 seconds (s) and then rinsed with aliquots of 100 μl of Milli-Q (ultrapure) water to remove unattached peptides. The sample on the mica surface was then air-dried for AFM observation. AFM was performed with Asylum-1 MFP-3D AFM System (Asylum Research, Santa Barbara, Calif.) using a tapping mode. The images utilized an Olympus Si tip (AC240FS). The cantilever's free resonance frequency was 70 kHz. Height images were recorded with 256×256 pixels resolution.

As shown in FIGS. 3 and 4, AFM morphological studies demonstrated that ST14 forms self-assembled nanofibers. Aggregates have been detected in T14, as shown in FIGS. 5 and 6.

Example 1

Atomic Force Microscopy (AFM) images of ST14 (SEQ ID NO:2) and T14 (SEQ ID NO:1) peptides were investigated to visualize their nano structures. Samples were prepared by placing an aliquot of approximately 50 microliters (μl) of the peptide (100 micromolar (μM)) solution on the surface (9 millimeters (mm) in diameter) of a mica surface. Each sample was left on the mica for about 30 seconds (s) and then rinsed with aliquots of 100 μl of Milli-Q (ultrapure) water to remove unattached peptides. The sample on the mica surface was then air-dried for AFM observation. AFM was performed with Asylum-1 MFP-3D AFM System (Asylum Research, Santa Barbara, Calif.) using a tapping mode. The images utilized an Olympus Si tip (AC240FS). The cantilever's free resonance frequency was 70 kHz. Height images were recorded with 256×256 pixels resolution.

As shown in FIGS. 3 and 4, AFM morphological studies demonstrated that ST14 (SEQ ID NO:2) forms self-assembled nanofibers. Aggregates have been detected in T14 (SEQ ID NO:1), as shown in FIGS. 5 and 6.