Meir Wilchek

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Meir Wilchek
Bar Ilan University and the Weizmann Institute of Science
Known forAffinity chromatography
AwardsWolf Prize, Israel Prize
Scientific career
FieldsBiochemist
InstitutionsWeizmann Institute of Science

Meir Wilchek (Hebrew: מאיר אשר וילצ'ק, born 17 October 1935) is an Israeli biochemist.[1] He is a professor at the Weizmann Institute of Science.

Early life and education

Meir Wilchek was born in

Mafdal and Meimad for the Knesset
.

Scientific contributions

Meir Wilchek is known for his research in the field of biorecognition or affinity phenomenon, and its various application, e.g. for affinity chromatography, affinity labeling, affinity therapy, and the avidin-biotin system. The avidin-biotin complex is the highest affinity interaction in nature, and its utilization to biochemistry integrates all of the former approaches.

Other contributions include conversion of serines to cysteines,[2] and was the first to prove experimentally the equation of Forster on dependence of energy transfer on distance,[3] an approach known today as FRET. He also studied the fine structure of these chromophores using circular dichroism.[4] More recently, he participated in a research team who studied how garlic works at the molecular level, thanks to a unique biotechnological procedure for producing large quantities of pure allicin, garlic's main biologically active component.[5]

Affinity chromatography

substrate, or receptor and ligand. The method was subsequently adopted for a variety of other techniques. Specific uses of affinity chromatography include antibody affinity, Immobilized metal ion affinity chromatography and purification of recombinant proteins - possibly the most common use of the method. To purify, proteins are tagged e.g. using His-tags or GST (glutathione-S-transferase) tags, which can be recognized by a metal ion ligand, such as imidazole
.

In 1971, Wilchek and colleagues applied this method to show that protein kinase is composed of regulatory and catalytic subunits.[7] In 1972, Wilchek showed that the method can be used to remove toxic compounds from blood, as exemplified by the removal of heme peptides from blood using immobilized human serum albumin, thus laying the grounds for modern hemoperfusion[8]

Affinity labeling

complementarity-determining regions (CDRs[9]
).

Affinity therapy

Affinity therapy, or

cytotoxic agent, allicin, in situ (at the site) of the cancer[11]

The avidin-biotin system

The avidin–biotin system is a technique for studying the interaction between two biomolecules in an indirect manner, as follows: Biotin is chemically coupled to a binder molecule (e.g., a protein, DNA, hormone, etc.) without disturbing the interaction with its target molecule; avidin is then used to “sandwich” between the biotinylated binder and a reporter molecule or probe. This allows for a variety of tasks, including localization and identification of the binder or target molecule. Consequently, the avidin-biotin system can frequently replace radioactive probes. Together with Ed Bayer, Wilchek established the Avidin-biotin system as a powerful tool in biological sciences. Early in the 1970s, they exploited Avidin as a probe and developed new methods and reagents to

ELISPOT and pull-down assays.[12]
More recently, Wilchek participated in structural studies of the avidin–biotin complex, to characterize the unique properties of this strong interaction. The studies have culminated in the determination of the
3D structure of the avidin–biotin complex by X-ray crystallography,[13] which aids in the design of specific artificial recognition sites.[14]

Honors and awards

See also

References

  1. ISBN 9780837911106
    . Retrieved 2014-12-13.
  2. doi:10.1021/bi00885a018.{{cite journal}}: CS1 maint: multiple names: authors list (link
    )
  3. PMID 6047638.{{cite journal}}: CS1 maint: multiple names: authors list (link
    )
  4. PMID 5687722.{{cite journal}}: CS1 maint: multiple names: authors list (link
    )
  5. ^ "Therapeutic Effects of Garlic Clarified by Weizmann Institute Research". Weizmann Institute of Science. 14 October 1997. Archived from the original on 8 November 2005.
  6. PMID 4971842
    .
  7. PMID 4332593.{{cite journal}}: CS1 maint: multiple names: authors list (link
    )
  8. PMID 4343271
    .
  9. PMID 5105033.{{cite journal}}: CS1 maint: multiple names: authors list (link
    )
  10. PMID 164279.{{cite journal}}: CS1 maint: multiple names: authors list (link
    )
  11. PMID 14707270.{{cite journal}}: CS1 maint: multiple names: authors list (link
    )
  12. PMID 3044183
    .
  13. PMID 8506353.{{cite journal}}: CS1 maint: multiple names: authors list (link
    )
  14. PMID 15079055.{{cite journal}}: CS1 maint: multiple names: authors list (link
    )
  15. ^ The Wolf Prize in Medicine Archived February 26, 2009, at the Wayback Machine
  16. ^ "Israel Prize Official Site - Recipients in 1990 (in Hebrew)".
  17. ^ Editor, ÖGV. (2015). Wilhelm Exner Medal. Austrian Trade Association. ÖGV. Austria.

External links

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