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Cover Picture: Proteolysis of Peptide Dendrimers (ChemBioChem 9/2009)
Author(s) -
Sommer Peter,
Fluxa Viviana S.,
Darbre Tamis,
Reymond JeanLouis
Publication year - 2009
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200990031
Subject(s) - proteolysis , chemistry , cleavage (geology) , dendrimer , trypsin , proteases , peptide , protease , chymotrypsin , stereochemistry , biochemistry , enzyme , biology , paleontology , fracture (geology)
The cover picture shows the discovery of proteolysis sites within peptide dendrimers. On p. 1527 ff. of this issue, J.‐L. Reymond et al. explain how proteolytic cleavage within the branches of these molecular trees was found to be possible by proteases such as trypsin (Trp) or chymotrypsin (Chy) when the correct amino acid (Arg for Trp, Phe for Chy) was placed at the cleavage site. Protease‐reactive dendrimers were identified by screening a one‐bead–one‐compound combinatorial library of dendrimers (top left) using an on‐bead proteolysis assay (red indicates the presence of free amino termini after proteolysis). It was also possible to hide proteolysis sites from the proteases by using a higher degree of branching in the dendrimers (not shown). A space‐filling rendering of a peptide dendrimer and its cleavage products upon trypsin cleavage is shown. Cover design and realization by Louise A. Reymond and Viviana S. Fluxa.