Amino Acid Functionalized Inorganic Nanoparticles as Cutting-Edge Therapeutic and Diagnostic Agents

Surfactant-like inorganic-organic hybrid molecules named as nanocrystallopolymers were designed by conjugation of the hydrophilic synthetic poly(amino acid), poly-α,β-(N-(2-hydroxyethyl)l-aspartamide), with hydrophobic inorganic nanoparticles. In aqueous media, amphiphilic nanocrystallopolymers form self-aggregates with unique morphologies. Here, a simple biolabeling method of nanocrystallopolymers was developed. Biotin was selected as a model biomolecule. The specific binding of biotin-labeled nanocrystallopolymers to the targeted surface was evaluated with a surface plasmon resonance sensor.

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The Binary Effect on Methicillin‐ResistantStaphylococcus aureusof Polymeric Nanovesicles Appended by Proline‐Rich Amino Acid Sequences and Inorganic Nanoparticles

Small ◽

10.1002/smll.201804247 ◽

2019 ◽

Vol 15 (18) ◽

pp. 1804247 ◽

Cited By ~ 3

Author(s):

Nicole J. Bassous ◽

Thomas J. Webster

Keyword(s):

Amino Acid ◽

Amino Acid Sequences ◽

Inorganic Nanoparticles

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Cutting Edge: IL-2–Induced Expression of the Amino Acid Transporters SLC1A5 and CD98 Is a Prerequisite for NKG2D-Mediated Activation of Human NK Cells

The Journal of Immunology ◽

10.4049/jimmunol.1700497 ◽

2017 ◽

Vol 199 (6) ◽

pp. 1967-1972 ◽

Cited By ~ 16

Author(s):

Helle Jensen ◽

Marc Potempa ◽

Dagmar Gotthardt ◽

Lewis L. Lanier

Keyword(s):

Amino Acid ◽

Nk Cells ◽

Cutting Edge ◽

Amino Acid Transporters ◽

Induced Expression

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Plastic Deformation in Microtomed Sections

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100066346 ◽

1971 ◽

Vol 29 ◽

pp. 458-459

Author(s):

J. Temple Black

Keyword(s):

Plastic Deformation ◽

Plastic Strain ◽

Applied Stress ◽

Elastic Strain ◽

High Strain ◽

Tool Material ◽

Cutting Edge ◽

Material Structure ◽

Geometrical Constraints

The output of the ultramicrotomy process with its high strain levels is dependent upon the input, ie., the nature of the material being machined. Apart from the geometrical constraints offered by the rake and clearance faces of the tool, each material is free to deform in whatever manner necessary to satisfy its material structure and interatomic constraints. Noncrystalline materials appear to survive the process undamaged when observed in the TEM. As has been demonstrated however microtomed plastics do in fact suffer damage to the top and bottom surfaces of the section regardless of the sharpness of the cutting edge or the tool material. The energy required to seperate the section from the block is not easily propogated through the section because the material is amorphous in nature and has no preferred crystalline planes upon which defects can move large distances to relieve the applied stress. Thus, the cutting stresses are supported elastically in the internal or bulk and plastically in the surfaces. The elastic strain can be recovered while the plastic strain is not reversible and will remain in the section after cutting is complete.

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The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100142372 ◽

1986 ◽

Vol 44 ◽

pp. 150-151

Author(s):

M.K. Lamvik ◽

L.L. Klatt

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Staining Pattern ◽

Banding Patterns ◽

Mass Thickness ◽

New Form

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.

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Electron probe x-ray microanalysis and electron microscopy of amino acid absorption and transport by the small intestine: inhibition by chemical poisons and correlation to the elemental composition of the epithelial cells

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100142311 ◽

1986 ◽

Vol 44 ◽

pp. 134-135

Author(s):

A. J. Tousimis

Keyword(s):

Small Intestine ◽

Amino Acid ◽

Epithelial Cells ◽

Elemental Composition ◽

Isotope Labeling ◽

Structural Components ◽

X Ray ◽

Human Small Intestine ◽

Transport Studies

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.

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Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100147776 ◽

1993 ◽

Vol 51 ◽

pp. 388-389

Author(s):

Chi-Ming Wei ◽

Margaret Hukee ◽

Christopher G.A. McGregor ◽

John C. Burnett

Keyword(s):

Amino Acid ◽

Natriuretic Peptide ◽

Vascular Tone ◽

Cardiac Tissue ◽

Ring Structure ◽

Terminal Amino Acid ◽

Amino Acid Peptide ◽

Normal Human ◽

Terminal Amino ◽

The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

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