Identification and characterization of peptide fragments for the direct and site-specific immobilization of functional proteins onto the surface of 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 as "elongation factor Tu (ELN)" via the peptide MS fingerprinting method.

Essential oil composition and antioxidant activities of Curcuma aromatica Salisb.

The chemical composition of the hydro-distilled essential oil from leaves of Curcuma aromatica Salisb. was analysed by GC-MS. Twenty-three compounds representing 94.

Tandem multimer expression of angiotensin I-converting enzyme inhibitory peptide in Escherichia coli.

It is common for small tandem peptide multimer genes to be indirectly inserted into expression vectors and fused with a protein tag. In this study, a multimer of the tandem angiotensin I-converting enzyme inhibitory peptide (ACE-IP) gene was directly transferred to a commercially available vector and the designed gene was expressed as a repeated peptide in Escherichia coli BL21(DE3)pLysS. The process further developed in our study was the construction of six-repeated ACE-IP synthetic genes and their direct insertion.