4.7 Article

Analytical platforms for activity-based protein profiling - exploiting the versatility of chemistry for functional proteomics

Journal

CHEMICAL COMMUNICATIONS
Volume -, Issue 22, Pages 2311-2319

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/b600653c

Keywords

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Funding

  1. NATIONAL CANCER INSTITUTE [R33CA118696, R01CA087660, R37CA087660] Funding Source: NIH RePORTER
  2. NATIONAL INSTITUTE ON DRUG ABUSE [R01DA015197, P01DA017259] Funding Source: NIH RePORTER
  3. NCI NIH HHS [R01 CA087660-06, R33 CA118696-01, CA087660, R33 CA118696, CA118696, R01 CA087660] Funding Source: Medline
  4. NIDA NIH HHS [R01 DA015197, P01 DA017259, P01 DA017259-02, DA015197, R01 DA015197-04, DA017259] Funding Source: Medline

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The field of proteomics aims to develop and apply technologies for the characterization of protein function on a global scale. Toward this end, synthetic chemistry has played a major role by providing new reagents to profile segments of the proteome based on activity rather than abundance. Small molecule probes for activity-based protein profiling have been created for more than a dozen enzyme classes and used to discover several enzyme activities elevated in disease states. These innovations have inspired complementary advancements in analytical chemistry, where new platforms have been introduced to augment the information content achievable in chemical proteomics experiments. Here, we will review these analytical platforms and discuss how they have exploited the versatility of chemical probes to gain unprecedented insights into the function of proteins in biological samples of high complexity.

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