Adsorption of human serum albumin onto highly orientated pyrolytic graphite surface studied by atomic force microscopy

Scanning ◽  
2015 ◽  
Vol 37 (2) ◽  
pp. 158-164 ◽  
Author(s):  
XIAO Peng ◽  
HAORAN Fu ◽  
Ruisi Liu ◽  
Lin Zhao ◽  
Yuangang Zu ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Pyrolytic Graphite ◽  
Graphite Surface ◽  
Force Microscopy ◽  
Atomic Force

Study of interaction between syringin and human serum albumin by multi-spectroscopic method and atomic force microscopy

2010 ◽  
Vol 983 (1-3) ◽  
pp. 133-140 ◽  
Author(s):  
Wenhua Gao ◽  
Nana Li ◽  
Yaowen Chen ◽  
Yanping Xu ◽  
Yuejuan Lin ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Spectroscopic Method ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Investigation of the Interaction between Patulin and Human Serum Albumin by a Spectroscopic Method, Atomic Force Microscopy, and Molecular Modeling

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Li Yuqin ◽  
You Guirong ◽  
Yang Zhen ◽  
Liu Caihong ◽  
Jia Baoxiu ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Spectroscopic Method ◽  
Quenching Mechanism ◽  
Force Microscopy ◽  
Atomic Force ◽  
Study Results

The interaction of patulin with human serum albumin (HSA) was studied in vitro under normal physiological conditions. The study was performed using fluorescence, ultraviolet-visible spectroscopy (UV-Vis), circular dichroism (CD), atomic force microscopy (AFM), and molecular modeling techniques. The quenching mechanism was investigated using the association constants, the number of binding sites, and basic thermodynamic parameters. A dynamic quenching mechanism occurred between HSA and patulin, and the binding constants (K) were 2.60 × 104, 4.59 × 104, and 7.01 × 104 M−1at 288, 300, and 310 K, respectively. Based on fluorescence resonance energy transfer, the distance between the HSA and patulin was determined to be 2.847 nm. TheΔG0,ΔH0, andΔS0values across various temperatures indicated that hydrophobic interaction was the predominant binding force. The UV-Vis and CD results confirmed that the secondary structure of HSA was altered in the presence of patulin. The AFM results revealed that the individual HSA molecule dimensions were larger after interaction with patulin. In addition, molecular modeling showed that the patulin-HSA complex was stabilized by hydrophobic and hydrogen bond forces. The study results suggested that a weak intermolecular interaction occurred between patulin and HSA. Overall, the results are potentially useful for elucidating the toxigenicity of patulin when it is combined with the biomolecular function effect, transmembrane transport, toxicological, testing and other experiments.

Atomic force microscopy of human serum albumin (HSA) on poly(styrene/acrolein) microspheres

1996 ◽  
Vol 274 (6) ◽  
pp. 513-519 ◽  
Author(s):  
D. Kowalczyk ◽  
J. -P. Marsault ◽  
S. Slomkowski
Keyword(s):  
Atomic Force Microscopy ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Force Microscopy ◽  
Atomic Force

The interaction of 2-mercaptobenzimidazole with human serum albumin as determined by spectroscopy, atomic force microscopy and molecular modeling

2013 ◽  
Vol 104 ◽  
pp. 311-317 ◽  
Author(s):  
Yuqin Li ◽  
Baoxiu Jia ◽  
Hao Wang ◽  
Nana Li ◽  
Gaopan Chen ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals The interaction of human serum albumin with titanium studied by means of atomic force microscopy

2008 ◽  
Vol 40 (3-4) ◽  
pp. 157-161 ◽  
Author(s):  
Isabel Van De Keere ◽  
Ronnie Willaert ◽  
Els Tourwé ◽  
Annick Hubin ◽  
Jean Vereecken
Keyword(s):  
Atomic Force Microscopy ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Force Microscopy ◽  
Atomic Force

Self-Assembled N-Succinyl-Chitosan Nanofibers for Reduced Protein Adhesion

2010 ◽  
Vol 76 ◽  
pp. 36-41
Author(s):  
Eyas Dayyoub ◽  
Udo Bakowsky
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Self Assembly ◽  
Adhesion Properties ◽  
Force Microscopy ◽  
Atomic Force ◽  
Biomaterial Surfaces ◽  
Force Curves ◽  
Protein Adhesion

Protein adhesion on biomaterial surfaces plays a major role in determining their biocompatibility and cell responses. The goal of this study was to produce chitosan-based coatings of implant material polyurethane (PUR) for reduced human serum albumin (HSA) adhesion. Succinic anhydride was employed for modifying chitosan and synthesis of N-succinyl-chitosan (NSCS) which was used as a matrix coating of PUR. NSCS showed self-assembly behaviour as nanofiber structures onto PUR surface. Atomic force microscopy (AFM) has emerged as useful tool for the molecular force measurements and therefore it has been chosen to investigate the adhesion properties of Human serum albumin (HSA) on the new matrix coatings and other three implant materials PUR, Silicon and Titanium. HSA molecules were covalently bound to the AFM tip by the use of cyanuric chloride as bivalent linker. Analyzing the force curves demonstrated the antiadhesive properties of the NSCS films in comparison with the uncoated PUR, Silicon and Titanium.

Human Serum Albumin Nanoparticles as a Carrier for On-Demand Sorafenib Delivery

2021 ◽  
Vol 22 ◽  
Author(s):  
Tania Caputo ◽  
Angela Maria Cusano ◽  
Menotti Ruvo ◽  
Anna Aliberti ◽  
Andrea Cusano
Keyword(s):  
Drug Delivery ◽  
Human Serum Albumin ◽  
Drug Release ◽  
Serum Albumin ◽  
Human Serum ◽  
Encapsulation Efficiency ◽  
Kinase Inhibitor ◽  
Force Microscopy ◽  
Atomic Force

Background: Drug delivery systems based on Human Serum Albumin (HSA) have been widely investigated due to their capability to interact with several molecules together with their nontoxicity, non-immunogenicity and biocompatibility. Sorafenib (SOR) is a kinase inhibitor used as the first-line treatment in hepatic cancer. However, because of its several intrinsic drawbacks (low solubility and bioavailability), there is a growing need for discovering new carriers able to overcome the current limitations. Objective: To study HSA particles loaded with SOR as a thermal responsive drug delivery system. Method: A detailed spectroscopy analysis of the HSA and SOR interaction in solution was carried out in order to characterize the temperature dependence of the complex. Based on this study, the synthesis of HSA particles loaded with SOR was optimized. Particles were characterized by Dynamic Light Scattering, Atomic Force Microscopy and by spectrofluorometer. Encapsulation efficiency and in vitro drug release were quantified by RP-HPLC. Results: HSA particles were monodispersed in size (≈ 200 nm); encapsulation efficiency ranged from 25% to 58%. Drug release studies that were performed at 37 °C and 50 °C showed that HS5 particles achieved a drug release of 0.430 µM in 72 hours at 50 °C in PBS buffer, accomplishing a 4.6-fold overall SOR release enhancement following a temperature increase from 37 °C to 50 °C. Conclusion: The system herein presented has the potential to exert a therapeutic action (in the nM range) triggering a sustained temperature-controllable release of relevant drugs.

Sign in / Sign up

Export Citation Format

Share Document