Morphological Analysis and Interaction of Chlorophyll and BSA

Gorza, Filipe D.S.; Pedro, Graciela C.; Trescher, Tarquin F.; Silva, Romário J. da; Silva, Josmary R.; Souza, Nara C. de

doi:10.1155/2014/872701

Cited by 10 publications

(8 citation statements)

References 35 publications

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“…The interaction of Chl with the protein stabilizing agent bovine serum albumin (BSA) was tested in a negative control experiment[9]. The fluorescent Chl a/lipid mixture was maintained constant, and Lil3.2 was exchanged with Glufibrinogen, a peptide standard used in mass spectrometry.…”

Section: Resultsmentioning

confidence: 99%

Lil3 dimerization and chlorophyll binding inArabidopsis thaliana

et al. 2015

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The two-helix light harvesting like (Lil) protein Lil3 belongs to the family of chlorophyll binding light harvesting proteins of photosynthetic membranes. A function in tetrapyrrol synthesis and stabilization of geranylgeraniol reductase has been shown. Lil proteins contain the chlorophyll a/b-binding motif; however, binding of chlorophyll has not been demonstrated. We find that Lil3.2 from Arabidopsis thaliana forms heterodimers with Lil3.1 and binds chlorophyll. Lil3.2 heterodimerization (25±7.8 nM) is favored relative to homodimerization (431±59 nM). Interaction of Lil3.2 with chlorophyll a (231±49 nM) suggests that heterodimerization precedes binding of chlorophyll in Arabidopsis thaliana.

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Section: Resultsmentioning

confidence: 99%

Lil3 dimerization and chlorophyll binding inArabidopsis thaliana

et al. 2015

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“…This fact has found practical application in some research and diagnostic methods of medicine and agriculture: the study of the interaction of biomolecules [5], the diagnosis of the patient's blood condition [6][7][8][9][10], the analysis of the quality of wheat grains [11,12] and carrot roots [13,14].…”

Section: анализ характеристик зигзагоподобных паттерновmentioning

confidence: 99%

“…Depending on the type of pattern or texture, various authors offered such evaluation criteria as: the number of optical density fluctuations [9] or the brightness distribution of the digital image [11] in circular sections of different diameters; the fractal dimension of Minkowski [5] and the local connected fractal dimension of the image [12]; parameters of gray-scale histograms at several scales [13][14][15]; the structural and spectral characteristics of an image region as a function of time [10].…”

Section: анализ характеристик зигзагоподобных паттерновmentioning

confidence: 99%

Characterization of zigzag patterns on the surface of bovine serum albumin films

Glibitskiy¹,

Gorobchenko²,

Ніколов³

et al. 2017

Biophysical Bulletin

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Analysis of the patterns formed during the drying of biological fluids is employed for research and diagnosis in medicine and agriculture. Saline solutions of native proteins and DNA are characterized by zigzag patterns, which could be quantitatively described using the specific length of zigzags L specific . The aim of this study was to analyze a wide number of characteristics in order to identify those most sensitive to the effects of various physical and chemical factors on the protein structure. We examined the films prepared from salt solutions of bovine serum albumin (BSA) under varying conditions, viz.: a proportional change in the concentration of the components, substitution of NaCl with NaF and NaBr, temperature treatment, gamma irradiation, and addition of trivalent iron and biologically active flavin mononucleotide. The results revealed that the distribution of zigzag segment lengths was approximately lognormal, and the distribution of angles between the segments was approximately logistic. Two parameters appeared to be the most informative, viz. the average length of the segments, mainly depending on Cl -concentration, and the number of segments, depending on: Cl -concentration, concentration of the non-aggregated (but not necessarily unfragmented) protein, and the excess concentration of ions and low molecular weight compounds. KEY WORDS: BSA, film, zigzag patterns, texture, statistical distribution. Аналіз патернів, що формуються при висиханні біологічних рідин, використовується для досліджень і діагностики в медицині і сільському господарстві. Для сольових розчинів нативних білків і ДНК характерні зигзагоподібні патерни, які можна кількісно описати за допомогою питомої довжини зигзагів L specific . У даній роботі ми аналізуємо розширений ряд характеристик цих патернів з метою виявити найбільш чутливі до дії різних фізичних і хімічних факторів на структуру білка. Були розглянуті плівки, отримані з сольових розчинів бичачого сироваткого альбуміну (БСА) при пропорційній зміні концентрації компонентів, заміні NaCl на NaF і NaBr, температурній обробці, гамма-опроміненні, а також додаванні тривалентного заліза і біологічно активної речовини -флавінмононуклеотида. Було визначено, що розподіл довжин сегментів зигзагів має близький до логнормального характер, а розподіл кутів між сегментами -близький до логістичного. Дані показали, що найбільш інформативними є два параметри: середня довжина сегментів, яка переважно залежить від концентрації Cl -, і кількість сегментів, яка залежить від концентрації Cl -, концентрації неагрегованого білка (але не обов'язково нефрагментованого), а також від надлишкової концентрації іонів і низькомолекулярних сполук. АНАЛІЗ ХАРАКТЕРИСТИК ЗИГЗАГОПОДІБНИХ ПАТЕРНІВКЛЮЧОВІ СЛОВА: БСА, плівка, зигзагоподібні патерни, текстура, статистичний розподіл.

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“…Interactions between bovine serum albumin and chlorophyll in aqueous solution under physiological conditions were conducted and found the binding constants, at different temperatures, indicating the low affinity of bovine serum albumin and chlorophyll 64 . In addition, chlorophyll may be affected by the pH in the systems with serum albumin 65 .…”

Section: Protein Bindingmentioning

confidence: 99%

“…In vitro interactions between bovine serum albumin and chlorophyll, in aqueous solution under physiological conditions, indicated "low affinity binding" of bovine serum albumin and chlorophyll 64 . Therefore, the interactions involving the plasma protein binding is likely to be minimal.…”

Section: Displacement Of Binding With Plasma Proteinsmentioning

confidence: 99%

Warfarin-chlorophyll herb-drug interactions

Siriwatanametanon¹

2017

Pharm Sci Asia

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Warfarin is one of the most commonly prescribed anticoagulants for preventing the formation of blood clots to reduce the risk of heart attack, stroke, deep vein thrombosis, and other serious conditions. Warfarin belongs to a group of vitamin K antagonists that has a narrow therapeutic index, slow onset of action and significant drug-drug, herb-drug interactions. Its unpredictable doseresponse relationship can increase risks of bleeding complications or inadequate anticoagulation. Consumption of foods and nutritional supplements rich in vitamin K can interfere with warfarin treatment because vitamin K can reduce the warfarin's effectiveness and potentially increase the risk of blood clots. There are chlorophyll products that are claimed to be beneficial to health when taken as a supplement in solid or liquid forms. Chlorophyll products are now increasingly distributed all over the world. These products make patients and healthcare providers confused about how they affect the effectiveness of warfarin treatment because they are derived from green vegetables, which have been known to cause significant herb-drug interactions. This review provides some information about chlorophylls and chlorophyll products that can potentially interact with warfarin, and some forms, such as chlorophyll drops or chlorophyll water, that can be taken safely because they contain the lowest amount of vitamin K.

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Morphological Analysis and Interaction of Chlorophyll and BSA

Cited by 10 publications

References 35 publications

Lil3 dimerization and chlorophyll binding inArabidopsis thaliana

Lil3 dimerization and chlorophyll binding inArabidopsis thaliana

Characterization of zigzag patterns on the surface of bovine serum albumin films

Warfarin-chlorophyll herb-drug interactions

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