Excited States of Fluorescent Proteins, mKO and DsRed: Chromophore−Protein Electrostatic Interaction Behind the Color Variations

Protein analysis can be used to efficiently detect the early stages of various diseases. However, conventional protein detection platforms require expensive or complex equipment, which has been a major obstacle to their widespread application. In addition, uncertain signals from non-specific adhesion interfere with the precise interpretation of the results. To overcome these problems, the development of a technique that can detect the proteins in a simple method is needed. In this study, a platform composed of gold nanoparticles (GNPs) was fabricated through a simple imprinting method for protein detection. The corrugated surface naturally formed by the nanoparticle assemblies simultaneously increases the efficiency of adhesion and binding with analytes and reduces undesired interactions. After forming the GNP micropatterns, post-functionalization with both cationic and neutral ligands was performed on the surface to manipulate their electrostatic interaction with proteins. Upon protein binding, the change in the electrical values of the micropatterns was recorded by using a resistance meter. The resistance of the positively charged micropatterns was found to increase due to the electrostatic interaction with proteins, while no significant change in resistance was observed for the neutral micropatterns after immersion in a protein solution. Additionally, the selective adsorption of fluorescent proteins onto the micropatterns was captured using confocal microscopy. These simply imprinted GNP micropatterns are sensitive platforms that can detect various analytes by measuring the electrical resistance with portable equipment.

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ÉTUDE THÉORIQUE DES PERTURBATIONS HOMOGÈNES : I. APPLICATION AUX INTERACTIONS Π–Π ET Δ–Δ DE NO

Canadian Journal of Physics ◽

10.1139/p66-142 ◽

1966 ◽

Vol 44 (8) ◽

pp. 1677-1683 ◽

Cited By ~ 45

Author(s):

P. Felenbok ◽

H. Lefebvre-Brion

Keyword(s):

Excited States ◽

Electrostatic Interaction ◽

Theoretical Interpretation ◽

Electron Configuration ◽

Overlap Integral ◽

Morse Functions ◽

Electronic Excited States ◽

Experimental Values ◽

Semi Empirical ◽

Lcao Mo

A theoretical interpretation of homogeneous perturbations is proposed for the case of two electronic excited states that differ strongly in electron configuration. The interaction parameter H can be expressed in terms of the vibrational overlap integral and the electrostatic interaction between the two states. In the case of the Π–Π and Δ–Δ interactions in the spectrum of the NO molecule, a semi-empirical calculation of this parameter is made, using Morse functions for the vibrational part and the LCAO-MO SCF function for the electronic part. The comparison with the "experimental" values given by Lagerqvist and Miescher supports this interpretation.

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Vuv Spectra Y to Mo

International Astronomical Union Colloquium ◽

10.1017/s0252921100107808 ◽

1988 ◽

Vol 102 ◽

pp. 239

Author(s):

M.S.Z. Chaghtai

Keyword(s):

Excited States ◽

Spectral Analyses ◽

Vuv Spectra

Using R.D. Cowan’s computations (1979) and parametric calculations of Meinders et al (1982), old analyses are thoroughly revised and extended at Aligarh, of Zr III by Khan et al (1981), of Nb IV by Shujauddin et Chaghtai (1985), of Mo V by Tauheed at al (1985). Cabeza et al (1986) confirmed the last one largely.Extensive studies have been reported of the 1–e spectra, Zr IV (Rahimullah et al 1980; Acquista and Reader 1980), Nb V (Shujauddin et al 1982; Kagan et al 1981) and Mo VI (Edlén et al 1985). Some interacting 4p54d2levels of these spectra have been reported from our laboratory, also.Detailed spectral analyses of transitions between excited states have furnished complete energy values for J ≠ 1 levels of these spectra during 1970s and 80s. Shujauddin et al (1982) have worked out Nb VI and Tauheed et al (1984) Mo VII from our lab, while Khan et al (1981) share the work on Zr V with Reader and Acquista (1979).

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Fluorescent proteins for in vivo imaging, where's the biliverdin?

Biochemical Society Transactions ◽

10.1042/bst20200444 ◽

2020 ◽

Vol 48 (6) ◽

pp. 2657-2667

Author(s):

Felipe Montecinos-Franjola ◽

John Y. Lin ◽

Erik A. Rodriguez

Keyword(s):

Hydrogen Peroxide ◽

In Vivo Imaging ◽

Near Infrared ◽

Fluorescent Protein ◽

Fluorescent Proteins ◽

Fluorescent Imaging ◽

Infrared Light ◽

Red Fluorescent Protein ◽

Color Palette

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.

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