[Illinois] ECE 416 Avidin-Biotin and Surface Functionalization I

By Brian Cunningham

University of Illinois at Urbana-Champaign

Published on

Abstract

           In this lecture, we start off by taking a look at X-Ray Crystallography and how it is used to understand how biomolecules binding works. The x-ray data is processed by computer algorithms to determine coordinates of all atoms in the protein. One type of binding this has been used to see is the advin-biotin binding. Advin is a highly stable glycoprotein that has four binding sites for biotin. Biotin is a small molecule essential for metabolic reactions to synthesize fatty acids and to metabolize leucine.The interaction between the two is the strongest interaction known that is not a covalent bond. It occurs because of the hydrophobic interactions between biotin and aromatic amino acids arranged inside advin binding pockets. It is widely used in biochem. applications because of its high specific and strong binding. Other functional groups may be added to the COOH part of biotin. Bifunctional linkers can link other molecules to advin. Because the biotin molecule is so small, it won't change the function of the larger molecule it is attached to. It can be attached to every type of biosensor and nanoparticle surface. It is also a standard test to simulate detection of protein-drug interactions. Streptavidin is a similar protein to avidin, but produced by bacteria rather than animals. It is often used in assays instead of avidin. There are other methods beside avidin-biotin linkages of surface functionalism that may produce better results in some aspects and are therefore used. These include adsorption, covalent bond linkages, and hydrogel. The driving force for adsorption is the hydrophobic effects, the Vander Waals forces, and the hydrogen bonding. The disadvantages are also discussed. Covalent linkages are then discussed and how they are the strongest attachment strength. They need to make chemical bond linkages between the sensor and protein. The lysine amino acids are the usual target. The lecture ends with a revision of amine functional groups that were discussed at the beginning of the semester.

Bio

My research group is focused on the application of sub-wavelength optical phenomena and fabrication methods to the development of novel devices and instrumentation for the life sciences. The group is highly interdisciplinary, with expertise in the areas of microfabrication, nanotechnology, computer simulation, instrumentation, molecular biology, and cell biology. In particular, we are working on biosensors based upon photonic crystal concepts that can either be built from low-cost flexible plastic materials, or integrated with semiconductor-based active devices, such as light sources and photodetectors, for high performance integrated detection systems.

Using a combination of micrometer-scale and nanometer-scale fabrication tools, we are devising novel methods and materials for producing electro-optic devices with nanometer-scale features that can be scaled for low-cost manufacturing. Many of our techniques are geared for compatibility with flexible plastic materials, leading to applications such as low cost disposable sensors, wearable sensors, flexible electronics, and flexible displays. Because our structures manipulate light at a scale that is smaller than an optical wavelength, we rely on computer simulation tools such as Rigorous Coupled Wave Analysis (RCWA) and Finite Difference Time Doman (FDTD) to model, design, and understand optical phenomena within photonic crystals and related devices.

In addition to fabricating devices, our group is also focused on the design, prototyping, and testing of biosensor instrumentation for high sensitivity, portability, and resolution. Advanced instruments enable high resolution imaging of biochemical and cellular interactions with the ability to monitor images of biochemical interactions as a function of time. Using the sensors and instrumentation, we are exploring new applications for optical biosensor technology including protein microarrays, biosensor/mass spectrometry systems, and microfluidics-based assays using nanoliter quantities of reagents. The methods and systems developed in the laboratory are applied in the fields of life science research, drug discovery, diagnostic testing, and environmental monitoring. -From Professor Cunningham's Faculty Profile

Cite this work

Researchers should cite this work as follows:

  • Brian Cunningham (2013), "[Illinois] ECE 416 Avidin-Biotin and Surface Functionalization I," https://nanohub.org/resources/17669.

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Time

Location

University of Illinois, Urbana-Champaign, IL

Submitter

NanoBio Node, Obaid Sarvana, George Michael Daley

University of Illinois at Urbana-Champaign

Tags

[Illinois] ECE 416 Lecture 29: Avidin-Biotin & Surface Functionalization I
  • Lecture 20: The Avidin-Biotin System 1. Lecture 20: The Avidin-Biotin … 0
    00:00/00:00
  • Reminder: Our Surface Functionalization Goals 2. Reminder: Our Surface Function… 33.21533923303835
    00:00/00:00
  • A Few Words on X-Ray Crystallography 3. A Few Words on X-Ray Crystallo… 77.974062004579878
    00:00/00:00
  • Xray Crystallography 4. Xray Crystallography 93.717632552404439
    00:00/00:00
  • A Few Words on X-Ray Crystallography 5. A Few Words on X-Ray Crystallo… 128.55183195349656
    00:00/00:00
  • Xray Crystallography 6. Xray Crystallography 307.557468733486
    00:00/00:00
  • Avidin 7. Avidin 496.10841994010923
    00:00/00:00
  • Avidin 8. Avidin 580.03280782103218
    00:00/00:00
  • Avidin+Biotin 9. Avidin+Biotin 666.80839351770294
    00:00/00:00
  • Biotin 10. Biotin 716.02254711995784
    00:00/00:00
  • Avidin-Biotin: Nature's Superglue 11. Avidin-Biotin: Nature's Superg… 825.7316804650344
    00:00/00:00
  • Avidin+Biotin 12. Avidin+Biotin 926.88722036286777
    00:00/00:00
  • Avidin-Biotin: Nature's Superglue 13. Avidin-Biotin: Nature's Superg… 1088.9096353707944
    00:00/00:00
  • Livnah Paper on Avidin-Biotin 14. Livnah Paper on Avidin-Biotin 1107.7523339792144
    00:00/00:00
  • Avidin-Biotin 15. Avidin-Biotin 1258.2459926017264
    00:00/00:00
  • Biotinylation 16. Biotinylation 1304.2370530209619
    00:00/00:00
  • Biotinylation 17. Biotinylation 1346.7570900123305
    00:00/00:00
  • Biotinylation 18. Biotinylation 1409.7313722036288
    00:00/00:00
  • Immobilizing a Protein 19. Immobilizing a Protein 1451.4359617840005
    00:00/00:00
  • Uses of Avidin-Biotin System 20. Uses of Avidin-Biotin System 1556.2581469085785
    00:00/00:00
  • Example Data 21. Example Data 1594.3154394926898
    00:00/00:00
  • Streptavidin (SA) 22. Streptavidin (SA) 1656.9178263167166
    00:00/00:00
  • Avidin-Biotin System 23. Avidin-Biotin System 1749.6437378897303
    00:00/00:00
  • Surface Functionalization Techniques 24. Surface Functionalization Tech… 1929.2692002818389
    00:00/00:00
  • Surface Functionalization Techniques 25. Surface Functionalization Tech… 2055.2177646644354
    00:00/00:00
  • Adsorption 26. Adsorption 2128.1092566496391
    00:00/00:00
  • Driving Forces for Adsorption 27. Driving Forces for Adsorption 2200.5048881451471
    00:00/00:00
  • Van Der Waals Forces 28. Van Der Waals Forces 2288.8920204333276
    00:00/00:00
  • H Bonds 29. H Bonds 2387.6922230051086
    00:00/00:00
  • The Problems with Adsorption 30. The Problems with Adsorption 2475.5834948035936
    00:00/00:00
  • Covalent Linkage 31. Covalent Linkage 2523.55799718161
    00:00/00:00
  • Bifunctional Linker 32. Bifunctional Linker 2602.5237801655803
    00:00/00:00
  • Common Surface States 33. Common Surface States 2646.4074335036112
    00:00/00:00
  • Common Funtional Groups: Amine 34. Common Funtional Groups: Amine 2711.3651576536904
    00:00/00:00
  • Amine acts at BASES 35. Amine acts at BASES 2758.2239739298925
    00:00/00:00