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AN10079809-20080930-0001  
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Title
Title Two-Dimensional crystal film of streptavidin : a binding base for biotinylated proteins for protein device application  
Kana  
Romanization  
Other Title
Title ストレプトアビジン2次元結晶膜によるビオチン化タンパク質の固定とデバイスへの応用  
Kana ストレプトアビジン 2ジゲン ケッショウマク ニ ヨル ビオチンカ タンパクシツ ノ コテイ ト デバイス エノ オウヨウ  
Romanization Sutoreputoabijin 2jigen kesshomaku ni yoru biochinka tanpakushitsu no kotei to debaisu eno oyo  
Creator
Name 古野, 泰二  
Kana フルノ, タイジ  
Romanization Furuno, Taiji  
Affiliation 慶應義塾大学医学部物理学教室  
Affiliation (Translated) Department of Physics, Keio University School of Medicine  
Role  
Link  
Edition
 
Place
横浜  
Publisher
Name 慶應義塾大学日吉紀要刊行委員会  
Kana ケイオウ ギジュク ダイガク ヒヨシ キヨウ カンコウ イインカイ  
Romanization Keio gijuku daigaku Hiyoshi kiyo kanko iinkai  
Date
Issued (from:yyyy) 2008  
Issued (to:yyyy)  
Created (yyyy-mm-dd)  
Updated (yyyy-mm-dd)  
Captured (yyyy-mm-dd)  
Physical description
 
Source Title
Name 慶應義塾大学日吉紀要. 自然科学  
Name (Translated) The Hiyoshi review of the natural science  
Volume  
Issue 44  
Year 2008  
Month  
Start page 1  
End page 17  
ISSN
09117237  
ISBN
 
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URI
 
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Doctoral dissertation
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Date of granted  
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Abstract
The two-dimensional crystal film of streptavidin (SA) has been prepared at the air/water interface and transferred onto hydrophobic silicon wafer. The transfer ratio has been improved from our previous studies, resulting in the entire covering of the surface of silicon wafer with 2D crystal domains of SA. Stable and controlled immobilization of biotinylated proteins in their active form is to be achieved on this SA surface. Binding of biotinylated protein G to the SA surface and thereafter immunoglobulin G (IgG) to this immobilized protein G have been demonstrated by atomic force microscopy (AFM) under water. The biotin-streptavidin linkage is so stable that the bound protein G/IgG complex withstands the lateral pressure of the AFM cantilever tip during scanning. The number of bound molecules can be counted directly in the AFM images, suggesting the possibility to develop an AFM-based protein device in which the binding assay is ensured at high signal to noise rarios. The present study achieved the densest packing of SA on a solid support compared with those using self assembled film of thiol molecules on gold or biotinylated lipid at the air/water interface, which so far led to a random packing of streptavidin molecules or scattered assembly of 2D crystal patches of SA on solid supports. As demonstrated in this paper, uniformity of the 2D crystal film of SA is essentially important for the binding assay by means of AFM.
 
Table of contents
Introduction
Experimental section
1. Materials.
2. Two-dimensional crystallization of SA
3. Atomic force microscopy
4. Immobilization of protein G/IgG complex on SA crystal surface
5. Effect of tween 20 on SA crystal structure
Results and discussion
1. 2D crystallization conditions
2. Nonspecific binding and stability of SA film
3. Immobilization of protein G/IgG complex onto SA crystal surface
4. Proposal for higher resolution imaging to discriminate the shape of immobilized proteins
5. Preservation of SA film.
6. Deposition of SA film onto glass or quartz plate
Conclusions
 
Keyword
Biotin  

AFM  

Protein G  

IgG  

Protein Array  

Protein Chip  
NDC
 
Note
創立150年記念号 : 自然科学のエッセンス = 150th anniversary number : essence of natural sciences

原著論文
 
Language
英語  
Type of resource
text  
Genre
Departmental Bulletin Paper  
Text version
 
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Last modified date
Oct 16, 2008 09:00:00  
Creation date
Oct 16, 2008 09:00:00  
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Index
/ Public / 日吉紀要 / 自然科学 / 44 (2008)
 
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