Resonance enhanced dynamic Rayleigh scattering

Stanton, Susan G.; Pecora, R.; Hudson, Bruce S.

doi:10.1063/1.442000

Cited by 110 publications

(60 citation statements)

References 25 publications

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“…The formation of the hydrophobic interface is helpful to the enhancement of the RRS signal. [33] 3. Other factors.…”

Section: Formation Of Ion-association Complex and Reasons Of The Enhamentioning

confidence: 99%

Study on the resonance Rayleigh scattering and resonance non‐linear scattering spectra of ion‐association complexes of [PdI₄]²⁻‐protein systems and their analytical applications

Luo¹,

Liu²,

Kong³

et al. 2009

Luminescence

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In an acid medium solution, proteins such as bovine serum albumin, human serum albumin, ovalbumin, hemoglobin, lysozyme, gamma-globulin, alpha-chymotrypsin and papain could react with [PdI(4)](2-) by virtue of electrostatic attraction and hydrophobic force to form ion-association complexes. As a result, the resonance Rayleigh scattering (RRS) and resonance nonlinear scattering such as second-order scattering (SOS) and frequency doubling scattering (FDS) intensities were enhanced greatly and new scattering spectra appeared. The maximum scattering peaks of RRS, SOS and FDS were at 367, 720 and 370 nm, respectively. The enhanced RRS, SOS and FDS intensities were directly proportional to the concentrations of proteins. The detection limits for the different proteins were 2.4-11.8 ng/mL for RRS method, 9.5-47.9 ng/mL for SOS method and 4.6-18.5 ng/mL for FDS method. In this work, the influences of the interaction of [PdI(4)](2-) with proteins on spectral characteristics of RRS, SOS and FDS were investigated and the optimum conditions were tested. Meanwhile, the effects of coexisting substances were tested and the results showed that the method exhibited a good selectivity. Based on the above research, a highly sensitive, simple and rapid method for the determination of trace amounts of proteins by resonance light scattering technique has been developed. It can be applied to the determination of proteins in tablet, human serum and urine samples.

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“…The formation of the hydrophobic interface is helpful to the enhancement of the RRS signal. [33] 3. Other factors.…”

Section: Formation Of Ion-association Complex and Reasons Of The Enhamentioning

confidence: 99%

Study on the resonance Rayleigh scattering and resonance non‐linear scattering spectra of ion‐association complexes of [PdI₄]²⁻‐protein systems and their analytical applications

Luo¹,

Liu²,

Kong³

et al. 2009

Luminescence

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“…Therefore, scattering intensity is greatly increased due to the resonance enhanced Rayleigh scattering effect. 38,39 (2) Enlargement of molecular volume. According to the Rayleigh scattering formula, 40 if the molecular …”

Section: Reasons For Rrs Enhancementmentioning

confidence: 99%

A Highly Sensitive Resonance Rayleigh Scattering Method for the Determination of Penicillin Antibiotics with Potassium Ferricyanide

Duan

Liu

et al. 2008

Chin. J. Chem.

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Heated in a boiling water bath, penicillin antibiotics such as amoxicillin, ampicillin, sodium cloxacillin, sodium carbenicillin and sodium benzylpenicillin could react with K 3 [Fe(CN) 6 ] to form combined products in a dilute HCl medium. As a result, resonance Rayleigh scattering (RRS) intensity was enhanced greatly and new RRS spectra appeared. The maximum scattering wavelengths of the five combined products are all located at 330 nm. The scattered intensity increments (∆I) of the combined products are directly proportional to the concentrations of the antibiotics in a certain range. The methods exhibit high sensitivity, and the detection limits for the five penicillin antibiotics are between 4.61 and 5.62 ng•mL -1 . The spectral characteristics of RRS and the optimum reaction conditions were investigated. The mechanism of reaction and the reasons for the enhancement of resonance light scattering were discussed. The effects of coexisting substances have been examined, and the results indicated that the method had a good selectivity. It can be applied to the determination of penicillin antibiotics in capsule, tablet, human serum and urine samples.

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“…Since there is a great difference on the shapes of transmission spectra of samples 1 and 2, a great difference on the bonding qualities of samples 1 and 2 can be further concluded. We think the gradient shape of transmission spectra of sample 1 is due to the Rayleigh scattering on the bonding interface [9] . The condition of Rayleigh scattering is the radius of particle r λ.…”

Section: Study On the Scattering Of The Bonding Interface Of The Compmentioning

confidence: 99%

Bonding quality of Yb:Y3Al5O12/Y3Al5O12 composite crystals

Wang

Zhao

et al. 2008

Sci. China Ser. E-Technol. Sci.

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Resonance enhanced dynamic Rayleigh scattering

Cited by 110 publications

References 25 publications

Study on the resonance Rayleigh scattering and resonance non‐linear scattering spectra of ion‐association complexes of [PdI₄]²⁻‐protein systems and their analytical applications

Study on the resonance Rayleigh scattering and resonance non‐linear scattering spectra of ion‐association complexes of [PdI₄]²⁻‐protein systems and their analytical applications

A Highly Sensitive Resonance Rayleigh Scattering Method for the Determination of Penicillin Antibiotics with Potassium Ferricyanide

Bonding quality of Yb:Y3Al5O12/Y3Al5O12 composite crystals

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Resonance enhanced dynamic Rayleigh scattering

Cited by 110 publications

References 25 publications

Study on the resonance Rayleigh scattering and resonance non‐linear scattering spectra of ion‐association complexes of [PdI4]2−‐protein systems and their analytical applications

Study on the resonance Rayleigh scattering and resonance non‐linear scattering spectra of ion‐association complexes of [PdI4]2−‐protein systems and their analytical applications

A Highly Sensitive Resonance Rayleigh Scattering Method for the Determination of Penicillin Antibiotics with Potassium Ferricyanide

Bonding quality of Yb:Y3Al5O12/Y3Al5O12 composite crystals

Contact Info

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Study on the resonance Rayleigh scattering and resonance non‐linear scattering spectra of ion‐association complexes of [PdI₄]²⁻‐protein systems and their analytical applications

Study on the resonance Rayleigh scattering and resonance non‐linear scattering spectra of ion‐association complexes of [PdI₄]²⁻‐protein systems and their analytical applications