Adsorption of human serum albumin onto highly orientated pyrolytic graphite surface studied by atomic force microscopy. Issue 2 (13th February 2015)

• Record Type: Journal Article
• Authors: Peng, XIAO; Fu, HAORAN; Liu, Ruisi; Zhao, Lin; Zu, Yuangang; Xu, Fengjie; Liu, Zhiguo
• Is Part Of: Scanning. Volume 37:Issue 2(2015)
• Page Start: 158
• Page End: 164
• Publication Date: 2015-02-13
• Subjects: Scanning electron microscopy -- Periodicals; 502.825
• DOI: 10.1002/sca.21193
• Languages: English
• ISSNs: 0161-0457

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Summary</title> <sec id="sca21193-sec-0001" sec-type="section"> <p>It is important to know the adsorption behavior and assembly structure of human serum albumin (HSA) molecules onto a carbonaceous substrate for further application of carbon nanomaterials in biomedical field. Individual HSA molecules and oligmers (dimer and trimer) adsorbed onto HOPG surface have been imaged by atomic force microscopy (AFM). Individual HSA molecule appeared as an ellipsoid on HOPG surface with average length of 12.6, width of 6.5, and height of 1.9 nm when they were incubated at the physiological condition (pH 7.4). HSA molecules also can form the interconnected chains, uniform network, and monolayer by tuning the initial concentrations and adsorption time. Furthermore, HSA molecules can assemble into quite different network structures and irregular chains at pH of 2, 5, and 10. This study could expand our knowledge of the interactions between protein and carbonaceous surfaces. SCANNING 37:158–164, 2015. © 2015 Wiley Periodicals, Inc.</p> </sec> </abstract>