Synthesis and characterisation of substrate-based peptides as inhibitors of histone demethylase KDM4C
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Synthesis and characterisation of substrate-based peptides as inhibitors of histone demethylase KDM4C. / Nielsen, Simon D; Leurs, Ulrike; Bergner, Magnus; Barris, Silvia Amor; Devkota, Kanchan; Meyer, Kamilla; Iaria, Daniella; McCaughan, Jack; Lohse, Brian; Kristensen, Jesper L; Clausen, Rasmus Prætorius.
In: Protein and Peptide Letters, Vol. 23, No. 9, 13.06.2016, p. 772 - 776.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Synthesis and characterisation of substrate-based peptides as inhibitors of histone demethylase KDM4C
AU - Nielsen, Simon D
AU - Leurs, Ulrike
AU - Bergner, Magnus
AU - Barris, Silvia Amor
AU - Devkota, Kanchan
AU - Meyer, Kamilla
AU - Iaria, Daniella
AU - McCaughan, Jack
AU - Lohse, Brian
AU - Kristensen, Jesper L
AU - Clausen, Rasmus Prætorius
PY - 2016/6/13
Y1 - 2016/6/13
N2 - The design and synthesis of modified pentapeptides based on a truncated version of the substrate for KDM4C, a histone lysine demethylase (KDM), and investigation of their inhibitory activity at KDM4C is reported. By modifying the lysine residue corresponding to lysine 9 at histone 3 (H3K9), three different series of peptides were designed and synthesized. One series contained N-acylated H3K9 and two series introduced triazoles in this position via click chemistry to enable facile variation of headgroups. As the click reaction is compatible with free amino acids this was performed on an azido containing deprotected pentapeptide, thus demonstrating a highly facile and convergent synthetic strategy for making substrate-based inhibitors. One of the 14 peptides showed inhibitory activity at KDM4C demonstrating the need for an iron chelator in the pentapeptide series.
AB - The design and synthesis of modified pentapeptides based on a truncated version of the substrate for KDM4C, a histone lysine demethylase (KDM), and investigation of their inhibitory activity at KDM4C is reported. By modifying the lysine residue corresponding to lysine 9 at histone 3 (H3K9), three different series of peptides were designed and synthesized. One series contained N-acylated H3K9 and two series introduced triazoles in this position via click chemistry to enable facile variation of headgroups. As the click reaction is compatible with free amino acids this was performed on an azido containing deprotected pentapeptide, thus demonstrating a highly facile and convergent synthetic strategy for making substrate-based inhibitors. One of the 14 peptides showed inhibitory activity at KDM4C demonstrating the need for an iron chelator in the pentapeptide series.
U2 - 10.2174/0929866523666160613210831
DO - 10.2174/0929866523666160613210831
M3 - Journal article
C2 - 27295953
VL - 23
SP - 772
EP - 776
JO - Protein and Peptide Letters
JF - Protein and Peptide Letters
SN - 0929-8665
IS - 9
ER -
ID: 162710545