scholarly journals Human Serum Albumin in the Presence of AGuIX Nanoagents: Structure Stabilisation without Direct Interaction

2020 ◽  
Vol 21 (13) ◽  
pp. 4673 ◽  
Author(s):  
Xiaomin Yang ◽  
Marta Bolsa-Ferruz ◽  
Laurent Marichal ◽  
Erika Porcel ◽  
Daniela Salado-Leza ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Intravenous Injection ◽  
Fluorescence Emission ◽  
Blood Stream ◽  
High Ratio ◽  
Blood Protein ◽  
Blood Proteins ◽  
The Impact

The gadolinium-based nanoagent named AGuIX® is a unique radiosensitizer and contrast agent which improves the performance of radiotherapy and medical imaging. Currently tested in clinical trials, AGuIX® is administrated to patients via intravenous injection. The presence of nanoparticles in the blood stream may induce harmful effects due to undesired interactions with blood components. Thus, there is an emerging need to understand the impact of these nanoagents when meeting blood proteins. In this work, the influence of nanoagents on the structure and stability of the most abundant blood protein, human serum albumin, is presented. Synchrotron radiation circular dichroism showed that AGuIX® does not bind to the protein, even at the high ratio of 45 nanoparticles per protein at 3 mg/L. However, it increases the stability of the albumin. Isothermal thermodynamic calorimetry and fluorescence emission spectroscopy demonstrated that the effect is due to preferential hydration processes. Thus, this study confirms that intravenous injection of AGuIX® presents limited risks of perturbing the blood stream. In a wider view, the methodology developed in this work may be applied to rapidly evaluate the impact and risk of other nano-products that could come into contact with the bloodstream.

scholarly journals 1723. Human Serum Albumin Regulates the Growth of Candida auris in vitro

2019 ◽  
Vol 6 (Supplement_2) ◽  
pp. S631-S632
Author(s):  
Jun Sakai
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Candida Species ◽  
Blood Protein ◽  
Albumin Concentration ◽  
Blood Proteins ◽  
Candida Auris ◽  
Xtt Assay ◽  
High Albumin

Abstract Background Candida auris is commonly detected in human ear secretions. However, C. auris occasionally causes bloodstream infections even in immunocompetent patients resulting in poor prognosis. It was speculated that C. auris growth within the blood might be regulated by proteins in the bloodstream. Thus, in this study, the potential role of blood proteins in the regulation of C. auris growth was investigated. Methods Five Candida species (C. albicans, C. auris, C. glabrata, C. parapsilosis, and C. tropicalis) were incubated overnight. Colony suspensions for each species were prepared and adjusted to OD 1.0 at absorbance 0.1. Then, human serum albumin (HSA) and bovine serum albumin (BSA) were diluted (2.5 g/dL–0.002 g/dL) and mixed with the suspensions. Mixed samples were adjusted to 100 μL and incubated on MHA plates at 35°C for 2 days. Then, 50 μL of the combined sample was extracted and streaked onto Yeast extract-Peptone-Dextrose (YPD) agar. The remaining 50 μL sample was analyzed using an XTT assay. Further testing was then conducted on the effects of a specific blood protein albumin on Candida. Thereby, C. albicans and C. auris were cultured following the procedure above and stained with Annexin V and PI. Results The growth of C. auris mixed with a high albumin concentration (2.5~0.15 g/dL) was regulated compared with that of other Candida species (P < 0.01) (Figures 1 and 2); however, the growth of C. auris mixed with a lower albumin concentration was similar to that of other species. The wash-out study showed that C. auris growth and survival in the high albumin concentration was not different than that of other species. Conclusion HSA and BSA regulated C. auris growth which led to increased necrosis of C. auris. Conversely, growth of the other Candida species was not regulated. Therefore, albumin might be involved in the growth and necrosis of C. auris. As the highest concentration at which albumin regulated C. auris growth was similar to that found in human serum, it is possible that serum albumin might help prevent C. auris from entering the bloodstream via the ear or skin. Disclosures All authors: No reported disclosures.

The effects of different anaesthetic agents on the estimation of uterine vascular permeability in mice

1988 ◽  
Vol 22 (4) ◽  
pp. 343-346 ◽  
Author(s):  
S. R. Milligan ◽  
C. Edwards
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Vascular Permeability ◽  
Intravenous Injection ◽  
Body Wall ◽  
Anaesthetic Agent ◽  
Vascular Studies ◽  
Anaesthetic Agents ◽  
Pentobarbitone Sodium

Vascular permeability in the uterus and other tissues of mice was assessed using the accumulation of 125I-human serum albumin 30 min after its intravenous injection. The anaesthetic agent employed for the 125I-albumin injection differentially affected the estimates of vascular permeability: intraperitoneal (i.p.) tribromoethanol of pentobarbitone sodium produced significantly higher values for the uterus and body wall than ether. The i.p. administration of either Saffan or pentobarbitone sodium reduced estimates of vascular permeability in the duodenum. These results emphasize the importance of the choosing a suitable anaesthetic agent in vascular studies of the uterus and other abdominal tissues.

scholarly journals Rapid identification of Human Serum Albumin binding peptides from a phage display library：a back-of-the-envelope assessment of positive binders using titer-based criteria

2015 ◽  
Author(s):  
Yi-Feng Shi ◽  
Min Li ◽  
Jia-Di Zhang ◽  
Lei Bian
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Phage Display ◽  
Human Serum ◽  
Half Life ◽  
Drug Carrier ◽  
Therapeutic Proteins ◽  
Blood Protein ◽  
Albumin Binding ◽  
Binding Peptides

Human serum albumin (HSA) is the most abundant protein in blood and has a 19-day in vivo half-life, the longest human blood protein. HSA has also been extensively studied as a drug carrier in a wide variety of clinical applications. HSA-binding, compared with HSA-fusion, is promising strategy for extending the plasma half-life of protein therapeutics. The construction of albumin-binding drugs requires assessment of a large enough quantity of HSA-binding peptide candidates for conjugation with therapeutic proteins. Here, we report a back-of-the-envelope assessment method to facilitate phage display selection of HSA-binding peptides. With an experimentally determined number of phage titers, we can calculate the specificity ratios and the recovery yields. The recovery yield is calculated using the titers of eluted phage divided by the titers of input phage. The specificity ratio is calculated using the titer of eluted phage from a target-coated plate divided by the titer of eluted phage from a blank-control plate. These parameters are defined as quantitative criteria for panning and characterization of binding phage clones. Consequently, this approach may enable more rapid and low-cost phage display screening of HSA-binding peptides, which could be used as candidates of HSA binders for conjugation with therapeutic proteins.

scholarly journals Spectroscopic Studies on the Interaction between Tilorone and Human Serum Albumin

2017 ◽  
Vol 5 (1) ◽  
pp. 48-59
Author(s):  
Alla Yegorova ◽  
Inna Leonenko ◽  
Yulia Scrypynets ◽  
Georgy Maltsev ◽  
Valery Antonovich ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Average Distance ◽  
Antiviral Drug ◽  
Fluorescence Emission ◽  
Resonance Energy ◽  
Spectroscopic Studies ◽  
Excitation Wavelength

Under physiological conditions, in vitro interaction between the antiviral drug 2,7-bis[2-(diethylamino)ethoxy]-9-fluorenone dihydrochloride (Tilorone, TIL) and human serum albumin (HSA) was investigated at excitation wavelength 280 nm and at different temperatures (298 K and 313 K) by fluorescence emission spectroscopy. TIL showed a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant is estimated as KA =7.19× 104L·mol-1 at 298 K. The enthalpy change (ΔHº) and entropy change (ΔSº) were derived to be negative values. A value of 1.63 nm for the average distance r between TIL (acceptor) and tryptophan residues of HSA (donor) was derived from the fluorescence resonance energy transfer.

DENATURATION OF HUMAN SERUM ALBUMIN BY CERIUM (III) CHLORIDE

2013 ◽  
Vol 08 (01n02) ◽  
pp. 59-71
Author(s):  
G. REZAEI BEHBAHANI ◽  
M. SHALBAFAN ◽  
N. GHEIBI ◽  
L. BARZEGAR ◽  
H. REZAEI BEHBAHANI ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Tertiary Structure ◽  
Fluorescence Emission ◽  
Titration Calorimetry ◽  
Tryptophan Residue ◽  
Spectroscopic Methods ◽  
Irreversible Denaturation

Cerium (III) Chloride-induced conformational changes of human serum albumin, HSA, in phosphate buffer, 10 mM at pH 7.4 was investigated, using isothermal titration calorimetry (ITC), UV and fluorescence emission spectroscopic methods. The results indicate that CeCl3, Ce3+, induces irreversible denaturation of the HSA structure. The UV absorption intensity of HSA + Ce3+ shows a slight blueshift in the absorbance wavelength with increasing Ce3+ concentration. The fluorescence intensity was increased regularly and a slight redshift was observed in the emission wavelength. The HSA + Ce3+ complex quenches the fluorescence of HSA and changes the microenvironment of tryptophan residue. The emission intensity increases suggesting the loss of the tertiary structure of HSA. The results obtained from the ITC data are in agreement with the spectroscopic methods. The strong negative cooperativity of Ce3+ binding with HSA (Table 1) recovered from the extended solvation model, indicates that HSA has been denatured as a result of its interaction with Ce3+ ions.

Elucidating the impact of glucosylation on human serum albumin: A multi-technique approach

2016 ◽  
Vol 92 ◽  
pp. 881-891 ◽  
Author(s):  
K.M. Neelofar ◽  
Jamal Ahmad ◽  
Zarina Arif ◽  
Khursheed Alam
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
The Impact

scholarly journals Rapid identification of Human Serum Albumin binding peptides from a phage display library：a back-of-the-envelope assessment of positive binders using titer-based criteria

2015 ◽  
Author(s):  
Yi-Feng Shi ◽  
Min Li ◽  
Jia-Di Zhang ◽  
Lei Bian
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Phage Display ◽  
Human Serum ◽  
Half Life ◽  
Drug Carrier ◽  
Therapeutic Proteins ◽  
Blood Protein ◽  
Albumin Binding ◽  
Binding Peptides

Human serum albumin (HSA) is the most abundant protein in blood and has a 19-day in vivo half-life, the longest human blood protein. HSA has also been extensively studied as a drug carrier in a wide variety of clinical applications. HSA-binding, compared with HSA-fusion, is promising strategy for extending the plasma half-life of protein therapeutics. The construction of albumin-binding drugs requires assessment of a large enough quantity of HSA-binding peptide candidates for conjugation with therapeutic proteins. Here, we report a back-of-the-envelope assessment method to facilitate phage display selection of HSA-binding peptides. With an experimentally determined number of phage titers, we can calculate the specificity ratios and the recovery yields. The recovery yield is calculated using the titers of eluted phage divided by the titers of input phage. The specificity ratio is calculated using the titer of eluted phage from a target-coated plate divided by the titer of eluted phage from a blank-control plate. These parameters are defined as quantitative criteria for panning and characterization of binding phage clones. Consequently, this approach may enable more rapid and low-cost phage display screening of HSA-binding peptides, which could be used as candidates of HSA binders for conjugation with therapeutic proteins.

scholarly journals Molecular mechanistic vision on binding interaction of triptan drug, a serotonin (5-HT1) agonist with human serum albumin through multispectral and computational assessments

2020 ◽  
Vol 11 (2) ◽  
pp. 145-155
Author(s):  
Manjushree Makegowda ◽  
Revanasiddappa Hosakere Doddarevanna
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Clinical Medicine ◽  
Fluorescence Emission ◽  
Binding Constants ◽  
Binding Interaction ◽  
Binding Ability ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

The triptan drug such as eletriptan in combination with hydrochloride (ETP) is a 5-HT1 receptor agonist used to treat the migraine headache. Human serum albumin (HSA), the fundamental serum protein, executes various functions, that includes transporting and binding of many ligands. HSA binding interaction with ETP is elucidated from molecular docking in composite with fluorescence (emission, 3D and synchronous), UV-vis and FT-IR spectroscopy at 296, 304 and 312 K (pH = 7.40). ETP after interaction modified the HSA secondary structure and its micro-environments. Energy transfer and thermodynamic parameters were evaluated. Various quenching and binding constants were computed for formed ETP-HSA complex. The dominant interactive forces for ETP and HSA binding are hydrogen bonds join up with van der Waals extent possibly at site III (IB). The presence of Ca2+, Co2+, Na+, Mg2+ and Fe3+ ions significantly affected binding ability of ETP towards HSA. The essentialness of this investigation is beneficial in life sciences, medicinal chemistry, pharmaceutical industry and clinical medicine.

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