Conformation of microcontact-printed proteins by atomic force miroscopy molecular sizing

被引：19
作者：
Biasco, A
Pisignano, D
Krebs, B
Pompa, PP
Persano, L
Cingolani, R
Rinaldi, R
机构：
[1] Univ Lecce, Natl Nanotechnol Lab, Ist Nazl Fis Mat, Dipartimento Ingn Innovaz, I-73100 Lecce, Italy
[2] Univ Lecce, ISUFI, Innovat Mat & Technol Sch, I-73100 Lecce, Italy
来源：
LANGMUIR | 2005年 / 21卷 / 11期
关键词：
D O I：
10.1021/la050010j
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
We investigated the structural changes occurring in proteins patterned via microcontact printing. This was done by molecular sizing using atomic force microscopy to observe the structure of printed individual metalloprotein molecules in the unlabeled and untreated states. We observed that the size of the printed proteins were more than 2-fold smaller than the native shape, which indicates that some deformations take place upon the contact-assisted adsorption on silanized silicon dioxide. This can be attributed to simultaneously occurring effects, and particularly to the sandwiching between surfaces of very different hydrophilic/hydrophobic properties during contact lithography.
引用
收藏
页码：5154 / 5158
页数：5
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