Fibrinogen (fg) molecules were observed to form very well organized patterns of nanofibrils by self-assembling on Au (1,1,1) surface without any addition of thrombin, growing in two orientations (longitude and transverse). This observation is new and unique for gold surfaces, in contrast with Mica or HOPG surfaces. Based on the experimental results, we proposed an assembly mechanism: Au-S interactions and its activated interactions in the 'αC-domain' are two main causes for the patterned assembly on Au(1,1,1) surface, and 'D: D' and 'γ XL ' interactions help the elongation and strengthening of the fibril assembly.Understanding protein adsorption on gold surface bears increasing importance for many reasons. 1 For example, colloidal gold and gold nanoparticles are finding very useful applications in disease treatment including as therapy for rheumatoid arthritis and Alzheimer's disease and as drug delivery carriers; 2 gold surface is widely used in label-free detection methods such as surface plasmon resonance; and gold materials are also used in the development of biosensors and tissue engineering scaffolds. 3 Due to its paramount role in blood coagulation and its high concentration in the blood, fibrinogen (fg) has been extensively investigated for its absorption on to different surfaces, 4-9 particularly for its surface-induced changes in conformation and bioactivity. However, the absorption of fg on gold surface is least investigated, lagging the advancement of gold nanoparticle studies for biomedical applications. Here we report our finding that fg self-assembly into highly ordered nano-fibrils in two growing orientation on bare Au(1,1,1) surface in the absence of thrombin, and propose a possible mechanism.We observed large variations of fg assembly patterns on Mica (Figure 1(a)), HOPG ( Figure 1(b)), and Au(1,1,1) (Figure 1(c)) surfaces. The samples were prepared and studied under the same conditions (4 μg/mL fg and 50 min incubation, see detailed methods in SI A). As shown in Figure 1(a), most fg molecules on the mica surface maintain its native trinodules structure, which was first proposed by Hall and Slayter. 10 The length of one molecule is about 50~60 nm, which is very close to the reported data. 7 In contrast to the mica surface, the HOPG surface was densely covered by an amorphous protein layer, which indicates that the hydrophobic HOPG surface has stronger adhesion to fg than the hydrophilic mica surface. A similar conclusion was also attained by Agnihotri 4 and Geer. 5 The isoelectric point of gold surface has been reported to be around pH 4.5, 11 indicating that the gold