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Front Cover: Molecular Epitope Determination of Aptamer Complexes of the Multidomain Protein C‐Met by Proteolytic Affinity‐Mass Spectrometry (ChemMedChem 4/2020)
Author(s) -
Lupu Loredana,
Wiegand Pascal,
Hüttmann Nico,
Rawer Stephan,
Kleinekofort Wolfgang,
Shugureva Irina,
Kichkailo Anna S.,
Tomilin Felix N.,
Lazarev Alexander,
Berezovski Maxim V.,
Przybylski Michael
Publication year - 2020
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.202000050
Subject(s) - aptamer , epitope , systematic evolution of ligands by exponential enrichment , chemistry , mass spectrometry , epitope mapping , computational biology , linear epitope , peptide , target protein , dna , selex aptamer technique , front cover , combinatorial chemistry , microbiology and biotechnology , chromatography , biophysics , biochemistry , antibody , cover (algebra) , biology , rna , genetics , mechanical engineering , engineering , gene
The Front Cover shows the interaction epitopes of the extracellular structure of human C‐Met receptor protein complexes with two DNA‐aptamers of 60 and 64 bases, produced in vitro by the SELEX ( S ystematic E volution of L igands by Ex ponential Enrichment) procedure. The C‐Met protein has been recently recognized as a highly useful biomarker in cancer diagnosis. Using proteolytic affinity–mass spectrometry in combination with SPR biosensor analysis, epitope identifications with high affinities were obtained for DNA aptamers with a single linear peptide (aptamer CLN0004; upper right), and a discontinuous assembled epitope (aptamer CLN0003; upper left). The molecular epitopes identified by mass spectrometry for the first time of DNA aptamers as potential antibody alternatives, render them of high interest for cellular diagnostics. More information can be found in the Full Paper by Loredana Lupu, Michael Przybylski et al. on page 363 in Issue 4, 2020 (DOI: 10.1002/cmdc.201900489).