Alginate as an antiglycating agent for human serum albumin

Sattarahmady, N.; Khodagholi, Fariba; Moosavi-Movahedi, Ali Akbar; Heli, H.; Hakimelahi, G. H.

doi:10.1016/j.ijbiomac.2007.01.015

Cited by 37 publications

(14 citation statements)

References 34 publications

(40 reference statements)

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“…Many studies discussed the structural changes and characteristics of proteins during the glycation process in vitro (11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)27), but the compatibility and confirmation of these properties with what occurs in vivo have not been approached. In order to deter mine whether the results of structural changes and characteristics of glycated albumin in vitro are compatible with those in the serum of diabetic patients, purification of albumin from the pool serum of normal and diabetic patients with different glucose blood concentrations was performed.…”

Section: Resultsmentioning

confidence: 99%

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A Biophysical Comparison of Human Serum Albumin to be Glycated In Vivo and In Vitro

Sattarahmady¹,

Moosavi-Movahedi²,

Habibi-Rezaei³

2011

Journal of Medical Biochemistry

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Kratak sadr`aj: Proces glikacije podrazumeva spajanje proteina sa hemijski reverzibilnim ranim proizvodima glikacije, Schiffovim bazama i Amadori aduktima. Spora i slo`ena prera spodela tih ranih proizvoda vodi stvaranju krajnjih produkata glikacije (AGEs) koji uti~u na komplikacije dijabetesa. Ovde su upore|ene biofizi~ke karakteristike in vitro i in vivo gliko zilisanog albumina u humanom serumu (HSA). Pro mene u sadr`aju a-heliksa, intenzitetu fluores cen cije specifi~ne za AGE, obimu modifikacije lizinskog ostatka i vrednosti povr{in skog napona, kao i formiranje Amadori produkata u HSA sli~ni su u in vitro i in vivo uslovima. Prime}eno je, me|utim, da su argininski ostaci pretrpeli modifikacije samo u fiziolo{ kim uslovima (in vivo), ali ne i in vitro. Ta razlika odnosi se na prisustvo 3-deoksi-glukozona, 1,2-dikarbo nilnog jedinjenja koje nastaje iz glukoze u fiziolo{kim uslo vima. Zaklju~ujemo da su rezultati biofizi~kih ispitivanja pro cesa glikacije HSA in vitro verodostojni.Klju~ne re~i: albumin u humanom serumu, glikacija, dijabeti~ari, argininski ostatak

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Section: Resultsmentioning

confidence: 99%

“…We have reported studies about the glycation of HSA in vitro and reported its characteristics and structural changes during the glycation process (19)(20)(21). In this study, the aim was to compare the structual cha racteristics of in vitro glycated human serum albumin with those of its counterpart in human serum.…”

Section: Introductionmentioning

confidence: 99%

A Biophysical Comparison of Human Serum Albumin to be Glycated In Vivo and In Vitro

Sattarahmady¹,

Moosavi-Movahedi²,

Habibi-Rezaei³

2011

Journal of Medical Biochemistry

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“…Circular dichroism (CD) is an excellent tool for studying secondary structure [39]. An extensive change in the secondary structure of proteins takes place after the glycation process; it means glycation induces α-helix to β-sheet transition that is detectable with circular dichroism (CD) [28,40]. The far-uv CD spectrum of HSA is characterized by the presence of two strong negative bands at 208 and 222 nm, which represent the helical characteristics of HSA [28].…”

Section: Discussionmentioning

confidence: 99%

“…The results were expressed as molar ellipticity [θ ], which is defined as [θ ] = θ millidegrees / {10 × number of amino acid (lc)}, where c is the molar concentration of the sample and l is the length of the light path (cm). The amount of secondary structure associated with the samples was calculated by CDNN software [28].…”

Section: Circular Dichroism (Cd) Experimentsmentioning

confidence: 99%

“…A Shimadzu UV-3100 spectrophotometer equipped with a water bath (±0.5 • C) was used for recording the spectrum changes of the HSA samples (1 mg/ml in 50 mM sodium phosphate buffer; pH 7.4 at 25 • C) in a wavelength range of 200-550 nm in presence of different papaverine concentrations for investigation of the interaction between papaverine and HSA [28].…”

Section: Uv-visible Experimentsmentioning

confidence: 99%

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Papaverine increases human serum albumin glycation

Ahmadzadeh

2014

J Biol Phys

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Glycation is a non-enzymatic reaction that is initiated by the primary addition of sugars to amino groups of proteins. In the early phase of glycation, the synthesis of intermediates leads to formation of Amadori compounds. In the last phase, advanced glycation end products (AGE) are irreversibly formed following a complex cascade of reactions. It has recently been shown that glycation also affects diabetes-related complications and Alzheimer's disease. In this study, human serum albumin at a concentration of 10 mg/ml was incubated in PBS with 40 mM of glucose and in different concentrations of papaverine (25, 100, 250, 500 µM) for 42 days at 37 • C. HSA with no additives as well as with glucose 40 mM were incubated as a control and as a glycated sample, respectively. Following the incubation, the samples were prepared for circular dichroism, fluorescence and absorbance techniques. The results showed that in presence of papaverine and glucose, the glycation of HSA increased notably compared with the glycated sample. In conclusion, in this work, we showed that papaverine affects HSA and increases its glycation level.

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Antioxidant Polymers: Metal Chelating Agents

Zalloum

Mubarak

2012

Antioxidant Polymers

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Antioxidants are generally used to retard the reaction of organic materials, such as synthetic polymers, with atmospheric oxygen. Such a reaction can cause the degradation of the polymer and can alter many of its properties. This in turn could lead to loss of flavor and the development of rancidity in foods, to an increase in viscosity and acidity, and to the formation of insolubles in lubricants. Natural polysaccharides -chitosan, chitin, and alginates -are biopolymers that are biodegradable, biocompatible, environmentally friendly, and nontoxic. Additionally, these polymers and many of their derivatives act as antioxidant materials; this is mainly attributed to the active hydroxyl and amino groups present in these biopolymers. Since chitosan, chitin, and alginates act as metal-chelating agents, this review will cover the existing and most recent literature on the use of these materials and their derivatives for this purpose, in addition to the synthetic methods for their derivatives, and their use as metal-chelating agents.

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Alginate as an antiglycating agent for human serum albumin

Cited by 37 publications

References 34 publications

A Biophysical Comparison of Human Serum Albumin to be Glycated In Vivo and In Vitro

A Biophysical Comparison of Human Serum Albumin to be Glycated In Vivo and In Vitro

Papaverine increases human serum albumin glycation

Antioxidant Polymers: Metal Chelating Agents

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