scholarly journals Development of Fluorescence Quenching Optical Sensors for High Explosives Degradation Monitoring Final Report CRADA No. TSB-1453-97

2000 ◽  
Author(s):  
Joe H. Satcher ◽  
Ron E. Varosh
Keyword(s):  
Fluorescence Quenching ◽  
Optical Sensors ◽  
Final Report ◽  
High Explosives ◽  
Degradation Monitoring

scholarly journals Sensing of Proteins by ICD Response of Iron(II) Clathrochelates Functionalized by Carboxyalkylsulfide Groups

Biomolecules ◽  
2020 ◽  
Vol 10 (12) ◽  
pp. 1602
Author(s):  
Mykhaylo Losytskyy ◽  
Nina Chornenka ◽  
Serhii Vakarov ◽  
Samuel M. Meier-Menches ◽  
Christopher Gerner ◽  
...  
Keyword(s):  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Optical Sensors ◽  
Tertiary Structure ◽  
Titration Calorimetry ◽  
Ionization Mass ◽  
Protein Fluorescence ◽  
Esi Ms ◽  
Promising Tool ◽  
Docking Calculations

Recognition of elements of protein tertiary structure is crucial for biotechnological and biomedical tasks; this makes the development of optical sensors for certain protein surface elements important. Herein, we demonstrated the ability of iron(II) clathrochelates (1–3) functionalized with mono-, di- and hexa-carboxyalkylsulfide to induce selective circular dichroism (CD) response upon binding to globular proteins. Thus, inherently CD-silent clathrochelates revealed selective inducing of CD spectra when binding to human serum albumin (HSA) (1, 2), beta-lactoglobuline (2) and bovine serum albumin (BSA) (3). Hence, functionalization of iron(II) clathrochelates with the carboxyalkylsulfide group appears to be a promising tool for the design of CD-probes sensitive to certain surface elements of proteins tertiary structure. Additionally, interaction of 1–3 with proteins was also studied by isothermal titration calorimetry, protein fluorescence quenching, electrospray ionization mass spectrometry (ESI-MS) and computer simulations. Formation of both 1:1 and 1:2 assemblies of HSA with 1–3 was evidenced by ESI-MS. A protein fluorescence quenching study suggests that 3 binds with both BSA and HSA via the sites close to Trp residues. Molecular docking calculations indicate that for both BSA and HSA, binding of 3 to Site I and to an “additional site” is more favorable energetically than binding to Site II.

Optical Sensors Based on Fluorescence Quenching

1993 ◽  
pp. 79-89 ◽  
Author(s):  
Wolfgang Trettnak
Keyword(s):  
Fluorescence Quenching ◽  
Optical Sensors

Optical sensors, 13: fibre-optic humidity sensor based on fluorescence quenching

1988 ◽  
Vol 15 (1) ◽  
pp. 77-83 ◽  
Author(s):  
Hermann E. Posch ◽  
Otto S. Wolfbeis
Keyword(s):  
Fluorescence Quenching ◽  
Optical Sensors ◽  
Humidity Sensor ◽  
Fibre Optic

scholarly journals Arc Initiation of High Explosives: Final Report

2011 ◽  
Author(s):  
J McCarrick ◽  
C Grant ◽  
V Tang ◽  
E Glascoe ◽  
J Zaug ◽  
...  
Keyword(s):  
Final Report ◽  
High Explosives
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