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Issue 1, 2006
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Immobilization of RNase S-Peptide on a single-stranded DNA-fixed gold surface and effective masking of its surface by an acridinyl poly(ethylene glycol)

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Abstract

Oligonucleotidepeptide conjugate 1 was synthesized by coupling of RNase S-peptide to a 24-mer single-stranded DNA (ssDNA) oligonucleotide to be immobilized on its complementary ssDNA oligonucleotide-fixed gold surface of sensor chip or electrode. Immobilization of 1 on the ssDNA-fixed gold surface through DNA duplex formation was confirmed by quartz crystal microbalance (QCM) and electrochemical measurements. After treating with a synthetic acridinyl poly(ethylene glycol) (APEG), specific interaction of S-protein with the S-peptide immobilized on the gold surface was demonstrated by QCM without nonspecific adsorption of unrelated proteins such as BSA and RNase A at the surfaces. This result suggested that the acridine parts of APEG could bind to the DNA duplex on the gold surface and the poly(ethylene glycol) parts were fastened on the surface to resist the adsorption of proteins. Thus, the combination of oligonucleotidepeptide conjugate, ssDNA-fixed chip and APEG with effective masking property provides a new tool for the analysis of specific peptideprotein interactions without disturbance by other unrelated proteins.

Graphical abstract: Immobilization of RNase S-Peptide on a single-stranded DNA-fixed gold surface and effective masking of its surface by an acridinyl poly(ethylene glycol)

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Publication details

The article was received on 09 Jun 2005, accepted on 08 Nov 2005 and first published on 23 Nov 2005


Article type: Paper
DOI: 10.1039/B508166A
Citation: Analyst, 2006,131, 55-61
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    Immobilization of RNase S-Peptide on a single-stranded DNA-fixed gold surface and effective masking of its surface by an acridinyl poly(ethylene glycol)

    K. Ohtsuka, K. Uemura, T. Nojima, M. Waki and S. Takenaka, Analyst, 2006, 131, 55
    DOI: 10.1039/B508166A

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