scholarly journals Properties of Different Varieties of Durian

2021 ◽  
Vol 11 (12) ◽  
pp. 5653
Author(s):  
Supeeraya Arsa ◽  
Angkana Wipatanawin ◽  
Rachit Suwapanich ◽  
Orachorn Makkerdchoo ◽  
Niphattha Chatsuwan ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Proteins ◽  
Natural Antioxidants ◽  
Scanning Calorimetry ◽  
Durio Zibethinus ◽  
Fluorescence Measurements ◽  
Novel Biomarkers ◽  
Artery Disease ◽  
First Time

Durian (Durio zibethinus Murr.), like many other exotic, tropical, and conventional fruits, is important in the prevention of different diseases. In this study, the characterization of the main bioactive compounds of the most popular cultivars of durian and their properties are described. The changes in the quality indices of the antioxidant status were determined by CUPRAC, ABTS, FRAP, DPPH, and ORAC assays. The profiling of phytochemicals was carried out by Fourier transform infrared (FTIR) spectroscopy and differential scanning calorimetry (DSC). For the first time, in vitro studies were performed by the interaction of extracted durian polyphenols with human serum proteins (HSP) such as human serum albumin (HSAlb), fibrinogen (HSFib) and globulin (HSGlo) as novel biomarkers of coronary artery disease (CAD). The fluorescence measurements of the resulting intensity and calculated binding properties of the interaction of polyphenols with proteins showed that the most reactive was Monthong durian cultivar. This study suggests that durian cultivars have relatively strong antioxidant, binding, and health potentials and could be a significant source of natural antioxidants used in daily fresh consumption and for functional foods.

scholarly journals Bioactivities of Phenolic Compounds from Kiwifruit and Persimmon

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4405
Author(s):  
Young-Mo Kim ◽  
Faridah Abas ◽  
Yong-Seo Park ◽  
Yang-Kyun Park ◽  
Kyung-Sik Ham ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Proteins ◽  
Antioxidant Properties ◽  
Fluorescence Measurements ◽  
3D Fluorescence Spectroscopy ◽  
Human Proteins ◽  
Artery Disease ◽  
Spectroscopy Studies ◽  
Human Serum Proteins

Fruit used in the common human diet in general, and kiwifruit and persimmon particularly, displays health properties in the prevention of heart disease. This study describes a combination of bioactivity, multivariate data analyses and fluorescence measurements for the differentiating of kiwifruit and persimmon, their quenching and antioxidant properties. The metabolic differences are shown, as well in the results of bioactivities and antioxidant capacities determined by ABTS, FRAP, CUPRAC and DPPH assays. To complement the bioactivity of these fruits, the quenching properties between extracted polyphenols and human serum proteins were determined by 3D-fluorescence spectroscopy studies. These properties of the extracted polyphenols in interaction with the main serum proteins in the human metabolism (human serum albumin (HSA), α-β-globulin (α-β G) and fibrinogen (Fgn)), showed that kiwifruit was more reactive than persimmon. There was a direct correlation between the quenching properties of the polyphenols of the investigated fruits with serum human proteins, their relative quantification and bioactivity. The results of metabolites and fluorescence quenching show that these fruits possess multiple properties that have a great potential to be used in industry with emphasis on the formulation of functional foods and in the pharmaceutical industry. Based on the quenching properties of human serum proteins with polyphenols and recent reports in vivo on human studies, we hypothesize that HSA, α-β G and Fgn will be predictors of coronary artery disease (CAD).

scholarly journals A Peptide Found in Human Serum, Derived from the C-Terminus of Albumin, Shows Antifungal Activity In Vitro and In Vivo

2020 ◽  
Vol 8 (10) ◽  
pp. 1627
Author(s):  
Tecla Ciociola ◽  
Pier Paolo Zanello ◽  
Tiziana D’Adda ◽  
Serena Galati ◽  
Stefania Conti ◽  
...  
Keyword(s):  
Antifungal Activity ◽  
Human Serum ◽  
Fungicidal Activity ◽  
Galleria Mellonella ◽  
Serum Proteins ◽  
Morphological Alterations ◽  
C Terminus ◽  
Different Sources

The growing problem of antimicrobial resistance highlights the need for alternative strategies to combat infections. From this perspective, there is a considerable interest in natural molecules obtained from different sources, which are shown to be active against microorganisms, either alone or in association with conventional drugs. In this paper, peptides with the same sequence of fragments, found in human serum, derived from physiological proteins, were evaluated for their antifungal activity. A 13-residue peptide, representing the 597–609 fragment within the albumin C-terminus, was proved to exert a fungicidal activity in vitro against pathogenic yeasts and a therapeutic effect in vivo in the experimental model of candidal infection in Galleria mellonella. Studies by confocal microscopy and transmission and scanning electron microscopy demonstrated that the peptide penetrates and accumulates in Candida albicans cells, causing gross morphological alterations in cellular structure. These findings add albumin to the group of proteins, which already includes hemoglobin and antibodies, that could give rise to cryptic antimicrobial fragments, and could suggest their role in anti-infective homeostasis. The study of bioactive fragments from serum proteins could open interesting perspectives for the development of new antimicrobial molecules derived by natural sources.

Reversible binding of 5- and 8-methoxypsoralen to human serum proteins (albumin) and to epidermis in vitro

1979 ◽  
Vol 101 (6) ◽  
pp. 669-677 ◽  
Author(s):  
M. ARTUC ◽  
G. STUETTGEN ◽  
W. SCHALLA ◽  
H. SCHAEFER ◽  
J. GAZITH
Keyword(s):  
Human Serum ◽  
Serum Proteins ◽  
Reversible Binding ◽  
Human Serum Proteins

scholarly journals Capacity of human serum to depolymerize actin filaments

Blood ◽  
1987 ◽  
Vol 70 (2) ◽  
pp. 524-530
Author(s):  
PA Janmey ◽  
SE Lind
Keyword(s):  
Human Serum ◽  
Actin Filaments ◽  
Serum Proteins ◽  
Normal Serum ◽  
Slow Phase ◽  
Rapid Phase ◽  
Plasma Gelsolin ◽  
Preferential Formation

Human blood depolymerizes filamentous (F-)actin. The interaction of actin filaments and monomers with human serum was studied by following the kinetics and extent of the depolymerization of pyrene-labeled F- actin and by analysis of serum proteins adhering to immobilized actin monomers. In physiologic Ca2+ concentrations, the depolymerization of F- actin proceeds in two stages: a rapid phase, attributed to direct severing of filaments by plasma gelsolin, and a slow phase attributed to the binding of actin monomers to vitamin D-binding protein (DBP). Without Ca2+, only the slow phase is observed. Human serum can completely depolymerize 10 to 18 mumol/L of actin, of which approximately 5 mumol/L occurs rapidly. Depolymerization can be accounted for by the normal serum concentrations of gelsolin and DBP. Fibrin(ogen) and fibronectin, which bind actin in vitro, do not contribute to the kinetics or extent of its depolymerization. Affinity chromatography and functional assays for the presence of gelsolin-actin complexes show that addition of G-actin to serum results in preferential formation of actin-DBP complexes, but that addition of F- actin to serum produces both gelsolin-actin complexes and DBP-actin complexes. The distinctive binding of actin monomers and polymers to these two serum proteins suggests a means by which their coordinated actions are maximized in vivo, from the standpoint of depolymerizing filaments and clearing monomers from the circulation.

A Differential Interaction of Doxorubicin and Daunorubicin with Human Serum Proteins

1981 ◽  
Vol 67 (5) ◽  
pp. 399-403 ◽  
Author(s):  
Franco Zunino ◽  
Romolo A. Gambetta ◽  
Adriano Zaccara ◽  
Roberto Carsana
Keyword(s):  
Human Serum ◽  
Reaction Mechanisms ◽  
Serum Proteins ◽  
Covalent Bond ◽  
Comparative Investigation ◽  
Experimental Conditions ◽  
Differential Interaction ◽  
Bound Drug ◽  
Human Serum Proteins

The results of a comparative investigation on the interaction of doxorubicin (adriamycin) and daunorubicin with serum proteins are reported. Whereas a strong interaction occurs in vitro between doxorubicin and human serum proteins, no appreciable binding to proteins could be detected for daunorubicin under similar experimental conditions. Since the protein-bound drug is only partially dissociated by physical procedures including gel-electrophoresis, column-chromatography and solvent extraction, the formation of a covalent bond is suggested. The doxorubicin binding to serum proteins is apparently nonselective for a class of proteins; it is strongly reduced in acid conditions and slightly dependent on the ionic strenght. Two tentative reaction mechanisms have been considered.

Effect of microencapsulated acetylsalicylic acid on glycosylation of human serum proteins in vitro

1990 ◽  
Vol 61 (3) ◽  
pp. 219-223 ◽  
Author(s):  
D JURETIC ◽  
I CEPELAK ◽  
V JALSENJAK ◽  
T ZANICGRUBISIC ◽  
K LIPOVAC ◽  
...  
Keyword(s):  
Acetylsalicylic Acid ◽  
Human Serum ◽  
Serum Proteins ◽  
Human Serum Proteins

scholarly journals Mangiferin Rich Products from Aphloia theiformis (Vahl) Benn Leaves: Extraction, Fractionation, Phytochemical Characterization, and Antioxidant Properties

Molecules ◽  
2020 ◽  
Vol 25 (9) ◽  
pp. 2081
Author(s):  
Dovilė Grauzdytė ◽  
Audrius Pukalskas ◽  
Chaker El Kalamouni ◽  
Petras Rimantas Venskutonis
Keyword(s):  
Antioxidant Capacity ◽  
Antioxidant Properties ◽  
Natural Antioxidants ◽  
Liquid Extraction ◽  
In Vitro Assays ◽  
Synthetic Antioxidant ◽  
Liquid Liquid Extraction ◽  
Extraction Solvents ◽  
First Time

Aphloia theiformis is traditionally used in Mauritius, Madagascar, and Reunion Island for treating several diseases. In this study, various extraction solvents and schemes were applied for the recovery of antioxidant rich fractions from the leaves of A. theiformis. The products were evaluated for their antioxidant capacity using well known in vitro assays. Major compounds were characterized by UPLC–QTOF–MS. Hydrophilic extracts of A. theiformis demonstrated strong antioxidant properties, which are comparable with the synthetic antioxidant Trolox. UPLC analysis confirmed mangiferin as the main secondary metabolite of A. theiformis. Tormentic and hydroxytormentic acids as well as their isomers were also abundant in A. theiformis extracts and fractions, while their amounts were determined for the first time. The most potential extract was further separated into the fractions by liquid-liquid extraction and by precipitation at low temperature. Antioxidant capacity and composition of secondary metabolites of derived fractions were determined. Some of the fractions possessed remarkable antioxidant capacity, comparable to pure mangiferin. The results obtained reveal high potential of A. theiformis for recovery of natural antioxidants and other bioactive phytochemicals, particularly mangiferin.

Adsorption of Human Serum Proteins on Carbonaceous Materials

2007 ◽  
Vol 336-338 ◽  
pp. 1814-1817
Author(s):  
B.G. Li ◽  
Yun Qing Kang ◽  
Guang Fu Yin ◽  
Chang Qiong Zheng
Keyword(s):  
Human Serum ◽  
Competitive Adsorption ◽  
Serum Proteins ◽  
Blood Compatibility ◽  
Carbon Film ◽  
Adsorption Ability ◽  
Rational Explanation ◽  
Labeling Method ◽  
Human Serum Proteins

In this paper, the adsorption of human serum albumin (HSA), human serum fibrinogen (HFG) and human serum immune globulin (IG) on surfaces of diamond like carbon film (DLC), diamond film (DF) and graphite has been studied. The adsorption isotherms of single component protein solution and the competitive adsorption of binary system have been investigated by radioisotope 125 I labeling method. Results showed that (1) the adsorptive amounts of HSA on DLC is more than that of HFG, but the adsorptive amounts of HFG on DF and graphite are apparently more than those HSA; (2) the relative competitive adsorption ability of three proteins on DF and graphite surfaces is HFG > IG > HSA, but that on DLC is HFG ≈ HAS > IG, comparison with HSA, there is no apparent competitive adsorption superiority on DLC for HFG. These results indicated that there is no apparent distinction for the adsorption of three human serum proteins on DLC, but the adsorption of HFG on DF and graphite takes precedence in varying degrees. It probably makes rational explanation for the result of blood-compatibility tests in vitro that DLC is good, but DF and graphite are worse.

scholarly journals Structural and electronic determinants of flavonoid binding to human serum albumin: an extensive ligand-based study

RSC Advances ◽  
2016 ◽  
Vol 6 (79) ◽  
pp. 75014-75022 ◽  
Author(s):  
Hrvoje Rimac ◽  
Željko Debeljak ◽  
Davor Šakić ◽  
Tin Weitner ◽  
Mario Gabričević ◽  
...  
Keyword(s):  
Density Functional Theory ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Density Functional ◽  
Density Functional Theory Calculations ◽  
Functional Theory ◽  
Flavonoid Aglycones ◽  
Fluorescence Measurements

The most prominent features responsible for binding of flavonoid aglycones to the IIA region of human serum albumin (HSA) were determined based onin vitrofluorescence measurements and density functional theory calculations.

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