Identification and Characterization of Peptides and Proteins in Doping Control Analysis

Mario      Thevis; Wilhelm      Schanzer

doi:10.2174/157016405774641147

Abstract

Analysis of peptides and proteins has become an important component of doping control laboratories. Several peptide hormones such as insulin, insulin-like growth factor-I, growth hormone, erythropoietin, and hemoglobin-based oxygen carriers are considered to possess an enormous potential to artificially increase athletic performance and belong to the list of prohibited compounds and methods established by regulatory authorities such as the World Anti-Doping Agency (WADA). In order to reveal abuse of those drugs in professional as well as amateur sports, doping control laboratories have been developing various strategies to identify target analytes in blood or urine specimens employing different biochemical techniques such as immunoaffinity purification, isoelectric focusing, gel electrophoresis, double-blotting as well as concomitant top-down and bottom-up mass spectrometry based proteomic approaches. These enable the qualitative determination of derivatives of naturally occurring peptides and proteins such as insulin and hemoglobin as well as possibilities to distinguish between endogenously produced and presumably identical recombinant proteins such as growth hormone and erythropoietin. Most applied strategies are common proteomics procedures, but they have been modified to meet the specific requirements and limitations of doping control, i.e. type of specimens, available amounts, required specificity and sensitivity, unambiguousness of results, and speed of analysis.

Keywords: Insulin, growth hormone, erythropoietin, oxygen carriers, doping, sport, mass spectrometry

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