Fabrication of DNA microarrays with poly(L-glutamic acid) monolayers on gold substrates for SPR imaging measurements.

نویسندگان

  • Yulin Chen
  • Anh Nguyen
  • Lifang Niu
  • Robert M Corn
چکیده

Robust single-stranded DNA (ssDNA) microarrays are created by attaching amine-modified oligonucleotides to a monolayer of poly(L-glutamic acid) (pGlu) that is electrostatically adsorbed onto a chemically modified gold thin film. This surface attachment chemistry methodology is first characterized with a combination of polarization-modulation Fourier transform infrared (PM-FTIR) spectroscopy and surface plasmon resonance (SPR) angle shift measurements. SPR imaging (SPRI) measurements of these ssDNA microarrays are then used to study two surface bioaffinity interactions: (i) the quantitative hybridization adsorption of complementary ssDNA onto mixed ssDNA microarray elements and (ii) the adsorption of single-stranded binding protein (SSB) onto fully and partially hybridized DNA microarray elements. The Langmuir adsorption coefficient (K(Ads)) of SSB binding to ssDNA was determined to be (5.5 +/- 0.4) x 10(9) M(-1).

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Fabrication of DNA microarrays on polydopamine-modified gold thin films for SPR imaging measurements.

Polydopamine (PDA) films were fabricated on thin film gold substrates in a single-step polymerization-deposition process from dopamine solutions and then employed in the construction of robust DNA microarrays for the ultrasensitive detection of biomolecules with nanoparticle-enhanced surface plasmon resonance (SPR) imaging. PDA multilayers with thicknesses varying from 1 to 5 nm were characteri...

متن کامل

Control of the Specific Adsorption of Proteins onto Gold Surfaces with Poly( L-lysine) Monolayers

Monolayers of the polypeptide poly(L-lysine) (PL) are used to control the specific adsorption of proteins onto gold surfaces. A PL monolayer modified with biotin is electrostatically adsorbed onto a vapor-deposited gold Eilm that has been coated with a self-assembled monolayer of the alkanethiol 1 1-mercaptoundecanoic acid (MUA). The immobilized biotin moieties act as specific adsorption sites ...

متن کامل

Surface plasmon resonance imaging measurements of protein interactions with biopolymer microarrays.

The surface-sensitive optical technique of surface plasmon resonance (SPR) imaging is an ideal method for the study of affinity binding interactions of unlabeled biological molecules in a multiplexed format. This approach has been widely applied to monitor DNA-DNA, DNA-RNA, peptide-protein, and protein-protein interactions as well as surface enzyme reactions. The success of SPR imaging measurem...

متن کامل

SPR imaging measurements of 1-D and 2-D DNA microarrays created from microfluidic channels on gold thin films.

Microfluidic channels fabricated from poly(dimethylsiloxane) (PDMS) are employed in surface plasmon resonance imaging experiments for the detection of DNA and RNA adsorption onto chemically modified gold surfaces. The PDMS microchannels are used to (i) fabricate "1-D" single-stranded DNA (ssDNA) line arrays that are used in SPR imaging experiments of oligonucleotide hybridization adsorption and...

متن کامل

Fabrication of histidine-tagged fusion protein arrays for surface plasmon resonance imaging studies of protein-protein and protein-DNA interactions.

The creation and characterization of histidine-tagged fusion protein arrays using nitrilotriacetic acid (NTA) capture probes on gold thin films for the study of protein-protein and protein-DNA interactions is described. Self-assembled monolayers of 11-mercaptoundecylamine were reacted with the heterobifunctional linker N-succinimidyl S-acetylthiopropionate (SATP) to create reactive sulfhydryl-t...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Langmuir : the ACS journal of surfaces and colloids

دوره 25 9  شماره 

صفحات  -

تاریخ انتشار 2009