Identification and characterization of peptide fragments for the direct and site-specific immobilization of functional proteins onto the surface of silicon nitride

• Published in: Journal of biotechnology Vol. 184; pp. 103 - 110
• Main Authors: Kumada, Yoichi, Ootsuka, Takeru, Asada, Masashi, Yoshizuka, Saori, Chiyama, Masateru, Sakane, Masayasu, Fida, Hasan M.D., Sawada, Kazuaki, Okumura, Koichi, Kishimoto, Michimasa
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 20.08.2014
• Subjects: Adsorption; Amino Acid Sequence; amino acid sequences; amino acids; Animals; Binding Sites; bioactive properties; Cattle; chymotrypsin; electrophoresis; Electrophoresis, Gel, Two-Dimensional; enzyme activity; Escherichia coli; Fragments; Glutathione S-transferase (GST); glutathione transferase; Glutathione Transferase - chemistry; Immobilization; Immobilized Proteins - chemistry; Material-binding peptide; Peptide Elongation Factor Tu - chemistry; Peptide Fragments - chemistry; Peptide Fragments - isolation & purification; Peptides; Proteins; Recombinant; Reflectometric interference spectroscopy (RIfS); reflectometry; Semiconductors; Sensors; Serum Albumin, Bovine - chemistry; Silicon Compounds - chemistry; Silicon nitride; spectroscopy; Surface chemistry; trypsin; Immobilization; Material-binding peptide; Glutathione S-transferase (GST); Reflectometric interference spectroscopy (RIfS); Silicon nitride

In this study, we successfully identified peptide fragments that have a strong affinity toward the surface of a silicon nitride (SiN) substrate. An E. coli soluble protein, which was preferentially adsorbed onto the surface of a SiN substrate was isolated by 2D electrophoresis, and it was identified...