SBIR-STTR Award

Vitrified Immobilized Proteins and Ligands
Award last edited on: 8/30/04

Sponsored Program
SBIR
Awarding Agency
NIH : NCRR
Total Award Amount
$832,688
Award Phase
2
Solicitation Topic Code
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Principal Investigator
Gary M Nishioka

Company Information

H & N Instruments Inc (AKA: H and N Instruments Inc)

219 North Westmoor Avenue Po Box 4338
Newark, OH 43055
   (740) 344-4351
   hni@infinet.com
   www.hninstruments.com
Location: Single
Congr. District: 12
County: Licking

Phase I

Contract Number: 1R43RR016833-01
Start Date: 00/00/00    Completed: 00/00/00
Phase I year
2002
Phase I Amount
$100,000
The overall objective of this research is to develop a new process and laboratory instrument capable of synthesizing microspots of vitrified immobilized proteins and ligands. Immobilized proteins and ligands stored in a vitrified (glassy) sugar matrix would be well preserved at room and even elevated temperatures. The ability to create such microspots could generate significant improvements in performance, cost, convenience, and storage requirements for applications requiring immobilized proteins and ligands. Examples of applications that could be improved include immunoassays, syntheses using immobilized enzymes, purifications involving affinity chromatography, and sensors using immobilized antibodies, enzymes, and ligands. We propose to use a microjet printer, designated SCAMP, to create vitrified microspots. We developed SCAMP as a laboratory instrument to print peptide microarrays. We propose to modify SCAMP to print protein/sugar solutions, and determine the conditions that yield vitrified microspots. The microspots printed would initially be of dimensions typical for an ink jet printer: 100 picoliters volume, creating a spot 60 - 100 micrometers in diameter. The advantages and drawbacks in using this technology will also be determined. PROPOSED COMMERCIAL APPLICATIONS: The proposed method could lead to improved immunoassays, syntheses using immobilized enzymes, purifications involving affinity chromatography, and sensors using immobilized antibodies, enzymes, and ligands.

Thesaurus Terms:
biomedical equipment development, immobilized enzyme, microarray technology, peptide chemical synthesis, preservation, protein structure function, technology /technique development affinity chromatography, enzyme linked immunosorbent assay, protein purification biotechnology

Phase II

Contract Number: 2R44RR016833-02
Start Date: 00/00/00    Completed: 00/00/00
Phase II year
2003
(last award dollars: 2004)
Phase II Amount
$732,688

The overall objective of this research is to develop a new process and laboratory instrument capable of synthesizing microspots of vitrified immobilized proteins and ligands. Immobilized proteins and ligands stored in a vitrified (glassy) sugar matrix would be well preserved at room and even elevated temperatures. The ability to create such microspots could generate significant improvements in performance, cost, convenience, and storage requirements for applications requiring immobilized proteins and ligands. Examples of applications that could be improved include immunoassays, syntheses using immobilized enzymes, purifications involving affinity chromatography, and sensors using immobilized antibodies, enzymes, and ligands.

Thesaurus Terms:
biomedical equipment development, immobilized enzyme, microarray technology, peptide chemical synthesis, preservation, technology /technique development affinity chromatography, enzyme linked immunosorbent assay, ligand, protein purification, protein structure function biotechnology