Cu(II)-Dependent degradation of DNA by riboflavin

Naseem, Imrana; Ahmed, M.Said; Bhat, Rashid; Hadi, S. M.

doi:10.1016/0278-6915(93)90209-h

Cited by 15 publications

(4 citation statements)

References 19 publications

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“…It can degrade a wide range of substrates by behaving as a photochemical sensitizer (15). Evidence from our laboratory and others have shown that riboflavin in the presence of Cu(II) and visible light can cause strand breakage in calf thymus DNA and supercoiled plasmid DNA (16) and fragmentation of proteins (17). Photoactivated riboflavin in its triplet-excited state reacts with molecular oxygen and generates reactive oxygen species (18).…”

mentioning

confidence: 99%

Riboflavin‐mediated cellular photoinhibition of cisplatin‐induced oxidative DNA breakage in mice epidermal keratinocytes

Husain

Naseem

2008

Photoderm Photoimm Photomed

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confidence: 99%

Riboflavin‐mediated cellular photoinhibition of cisplatin‐induced oxidative DNA breakage in mice epidermal keratinocytes

Husain

Naseem

2008

Photoderm Photoimm Photomed

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“…Pattison et al. (2012) suggested that peroxides formed on histidine and tryptophan residues resulted in subsequent peptide cleavage via damage transfer within a protein. In fact, Mao (2019) observed the formation of peptides in milk powder after IPL treatment (38.1 J/cm 2 ).…”

Section: Resultsmentioning

confidence: 99%

“…Another possible explanation for enhanced umami taste may be ribonucleotides arising from DNA fragmentation. Naseem et al (1993) reported that there was the degradation of DNA upon exposure to fluorescent light for 2 ho and that the degradation became more intense in the presence of riboflavin. They further explained that superoxide anion radicals and triplet state riboflavin interacted with the guanine base, leading to DNA breakage.…”

Section: Discussionmentioning

confidence: 99%

The effect of intense pulsed light on the sensory properties of nonfat dry milk

Kang

Chen

Ruan

et al. 2021

Journal of Food Science

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Our objectives were to examine (1) how intense pulsed light (IPL) processing parameters (exposure time and initial temperature) affected aroma, flavor, and mouthfeel of nonfat dry milk, (2) which levels of each parameter produced aroma, flavor, and mouthfeel changes from an untreated control sample, and (3) whether minimal or intense processing conditions produced a noticeable appearance change from the control. Four exposure times (1, 2, 3, and 4 passes through the IPL chamber) and three initial temperatures (25, 30, and 35°C) were studied with untreated milk powder as the control. The samples were prepared as both milk powder and reconstituted milk for sensory evaluation. Using standard evaluating protocols, trained descriptive analysis panelists rated the aroma, flavor, and mouthfeel of these samples. Panelists compared the appearance of the IPL-treated samples that underwent a minimal or intense processing condition to the control by using a two-out-of-five difference test. Increasing the exposure time led to increased intensities of overall flavor, burnt flavor, and umami taste in both milk powder and reconstituted milk, while increasing temperature increased animal and sulfur aromas in reconstituted milk only. Compared to the control, all levels of exposure time at any initial temperature resulted in increased aroma and flavor including cardboard aroma, sulfur aroma, and brothy flavor in both milk powder and reconstituted milk. Only the 4-pass exposure at the initial temperature of 25°C changed the appearance of milk powder. However, the appearance change was not noticeable in reconstituted milk. Practical Application:The standard evaluation protocols and lexicons provide useful tools for research on milk powder. Additionally, the understanding of critical factors impacting sensory properties will contribute to a better implementation of this decontamination technology.

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“…Riboflavin in the presence of Cu(II) and light causes breakage of calf thymus DNA and super coiled plasmid DNA [6], degradation of bovine serum albumin (BSA) [7], and hemolysis of red blood cells (RBC) [8]. Several reports have shown that photoactivated riboflavin reacts with molecular oxygen to generate reactive oxygen species (ROS) [9,10].…”

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confidence: 99%

Hemolysis of Human Red Blood Cells by Riboflavin-Cu(II) System: Enhancement by Azide

Ali

Sakhnini

Naseem

2005

Biochemistry (Moscow)

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Photoactivated riboflavin in the presence of Cu(II) generates reactive oxygen species (ROS) which can hemolyze human red blood cells (RBC). In the present work we examined the effect of sodium azide (NaN3) on RBC in the presence of riboflavin and Cu(II). The addition of NaN3 to the riboflavin-Cu(II) system enhanced K+ loss and hemolysis. The extent of K+ loss and hemolysis were time and concentration dependent. Bathocuproine, a Cu(I)-sequestering agent, inhibited the hemolysis completely. Among various free radical scavengers used to identify the major ROS involved in the reaction, thiourea was found to be the most effective scavenger. Thiourea caused almost 85% inhibition of hemolysis suggesting that *OH is the major ROS involved in the reaction. Using spectral studies and other observations, we propose that when NaN3 is added to the riboflavin-Cu(II) system, it inhibits the photodegradation of riboflavin resulting in increased *OH generation. Also, the possibility of azide radical formation and its involvement in the reaction could not be ruled out.

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Cu(II)-Dependent degradation of DNA by riboflavin

Cited by 15 publications

References 19 publications

Riboflavin‐mediated cellular photoinhibition of cisplatin‐induced oxidative DNA breakage in mice epidermal keratinocytes

Riboflavin‐mediated cellular photoinhibition of cisplatin‐induced oxidative DNA breakage in mice epidermal keratinocytes

The effect of intense pulsed light on the sensory properties of nonfat dry milk

Hemolysis of Human Red Blood Cells by Riboflavin-Cu(II) System: Enhancement by Azide

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