Quantification of the kinetics and thermodynamics of protein adsorption using atomic force microscopy

2005 ◽  
Vol 72A (3) ◽  
pp. 246-257 ◽  
Author(s):  
Robert T. T. Gettens ◽  
Zhijun Bai ◽  
Jeremy L. Gilbert
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Adsorption ◽  
Kinetics And Thermodynamics ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Lectins at Interfaces—An Atomic Force Microscopy and Multi-Parameter-Surface Plasmon Resonance Study

Materials ◽  
2018 ◽  
Vol 11 (12) ◽  
pp. 2348 ◽  
Author(s):  
Katrin Niegelhell ◽  
Thomas Ganner ◽  
Harald Plank ◽  
Evelyn Jantscher-Krenn ◽  
Stefan Spirk
Keyword(s):  
Atomic Force Microscopy ◽  
Surface Plasmon Resonance ◽  
Protein Adsorption ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Resonance Spectroscopy ◽  
Carbohydrate Binding ◽  
Force Microscopy ◽  
Atomic Force ◽  
Slow Kinetics

Lectins are a diverse class of carbohydrate binding proteins with pivotal roles in cell communication and signaling in many (patho)physiologic processes in the human body, making them promising targets in drug development, for instance, in cancer or infectious diseases. Other applications of lectins employ their ability to recognize specific glycan epitopes in biosensors and glycan microarrays. While a lot of research has focused on lectin interaction with specific carbohydrates, the interaction potential of lectins with different types of surfaces has not been addressed extensively. Here, we screen the interaction of two specific plant lectins, Concanavalin A and Ulex Europaeus Agglutinin-I with different nanoscopic thin films. As a control, the same experiments were performed with Bovine Serum Albumin, a widely used marker for non-specific protein adsorption. In order to test the preferred type of interaction during adsorption, hydrophobic, hydrophilic and charged polymer films were explored, such as polystyrene, cellulose, N,-N,-N-trimethylchitosan chloride and gold, and characterized in terms of wettability, surface free energy, zeta potential and morphology. Atomic force microscopy images of surfaces after protein adsorption correlated very well with the observed mass of adsorbed protein. Surface plasmon resonance spectroscopy studies revealed low adsorbed amounts and slow kinetics for all of the investigated proteins for hydrophilic surfaces, making those resistant to non-specific interactions. As a consequence, they may serve as favorable supports for biosensors, since the use of blocking agents is not necessary.

scholarly journals Nonspecific Protein Adsorption at the Single Molecule Level Studied by Atomic Force Microscopy

Langmuir ◽  
2007 ◽  
Vol 23 (20) ◽  
pp. 9921-9923 ◽  
Author(s):  
Peter Schön ◽  
Martin Görlich ◽  
Michiel J. J. Coenen ◽  
Hans A. Heus ◽  
Sylvia Speller
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Adsorption ◽  
Single Molecule ◽  
Single Molecule Level ◽  
Force Microscopy ◽  
Atomic Force ◽  
Nonspecific Protein Adsorption

Quantitative Analysis of Protein Adsorption via Atomic Force Microscopy and Surface Plasmon Resonance

2008 ◽  
Vol 8 (12) ◽  
pp. 1126-1134 ◽  
Author(s):  
Eva Servoli ◽  
Devid Maniglio ◽  
Maria Rosa Aguilar ◽  
Antonella Motta ◽  
Julio San Roman ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Surface Plasmon Resonance ◽  
Quantitative Analysis ◽  
Protein Adsorption ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Force Microscopy ◽  
Atomic Force

Adsorption Behaviour of Creatine Phosphokinase onto Silicon Wafers: Comparison between Ellipsometric and Atomic Force Microscopy Data

2005 ◽  
Vol 11 (S03) ◽  
pp. 56-60 ◽  
Author(s):  
S. M. Pancera ◽  
H. Gliemann ◽  
D. F. S. Petri ◽  
T. Schimmel
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Adsorption ◽  
Conformational Changes ◽  
Creatine Phosphokinase ◽  
Silicon Wafers ◽  
Adsorption Behaviour ◽  
Irreversible Adsorption ◽  
Force Microscopy ◽  
Atomic Force ◽  
Microscopy Data

Protein adsorption plays a major role in a variety of important technological and biological processes [1-2] and the understanding of the fundamental factors that determine protein adsorption are imperative to the development of biocompatible materials and biotechnological devices [3-4] as for example biosensors [5]. The adsorption of proteins on surfaces is a complex process. Due to the large size and different shapes of these adsorbing particles, the interactions between the adsorbed proteins on the surface can be strongly influentiated by the fact that the particles may undergo conformational changes upon adsorption [6-7]. In a previous work the adsorption behaviour of creatine phosphokinase (CPK) onto hydrophilic (silicon wafers and amino-terminated surfaces) and hydrophobic (Polystyrene, PS, coated wafers) substrates was investigated by means of null-ellipsometry and contact angle measurements [8]. This previous ellipsometric study led to a model, where CPK adsorption takes place in four stages: (i) a diffusive one, where all the arriving biomolecules are immediately adsorbed; (ii) the arriving biomolecules might stick on the latter and afterward diffuse to the free sites on the substrate, followed by conformational changes [6-7], (iii) formation of a monolayer and (iv) continuous and irreversible adsorption. A multilayer system might be formed, as well as aggregation processes might play a role at this stage. In this work Atomic Force Microscopy (AFM) measurements under water were done in order to confirm this four steps model and to observe changes in the film topography and homogeneity along the adsorption process. The thickness of the adsorbed CPK biofilm obtained by ellipsometry was also compared with that obtained by the wet AFM method.

scholarly journals Nanopatterns of polymer brushes for understanding protein adsorption on the nanoscale

RSC Advances ◽  
2014 ◽  
Vol 4 (85) ◽  
pp. 45059-45064 ◽  
Author(s):  
Xiaowen Wang ◽  
Rüdiger Berger ◽  
Jagoba Iturri Ramos ◽  
Tao Wang ◽  
Kaloian Koynov ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Adsorption ◽  
Polymer Brushes ◽  
Force Microscopy ◽  
Atomic Force ◽  
Adsorption Desorption

Nanopatterns of polymer brushes enable us to directly image protein adsorption/desorption processes on the polymer brushes by atomic force microscopy (AFM).

Atomic Force Microscopy Investigation of Protein Adsorption on Hydrogenated Amorphous Carbon

2013 ◽  
Vol 1527 ◽  
Author(s):  
Muhammad Zeeshan Mughal ◽  
Patrick Lemoine ◽  
Gennady Lubarsky
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Adsorption ◽  
Amorphous Carbon ◽  
Phosphate Buffer ◽  
Adsorbed Layer ◽  
Force Curve ◽  
Hydrogenated Amorphous Carbon ◽  
Force Microscopy ◽  
Atomic Force ◽  
Hydrogenated Amorphous

ABSTRACTProtein adsorption is the first phenomenon which occurs at nanoscale level when a given surface came into contact with a living fluid cell such as blood. Investigation of this adsorption at nanoscale provides useful information about kinetics and mechanism of conformation of proteins on a given surface. The present study investigates the adsorption of proteins using tapping/intermittent mode atomic force microscopy (T-AFM). The approach taken here is that hydrogenated amorphous carbon coating (a-C:H) is used as a model surface because it is amorphous, smooth, inert and hydrophobic. Two proteins namely albumin and fibrinogen in phosphate buffer (PBS) and de-ionized water are drop casted to study the adsorption kinetics. First and second resonance AFM data was used to investigate the adsorbed layer of proteins. AFM force curve and scratch experiment were used to verify the adhesion and thickness of the adsorbed layer. Combination of height, phase images along with the AFM force curve and scratch experiment shows inhomogeneous distribution of albumin protein in phosphate buffer compared to other protein solutions.

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