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A caged sperm‐activating peptide that has a photocleavable protecting group on the backbone amide
Author(s) -
Tatsu Yoshiro,
Nishigaki Takuya,
Darszon Alberto,
Yumoto Noboru
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03000-4
Subject(s) - side chain , peptide , amide , chemistry , sperm , intracellular , stereochemistry , receptor , combinatorial chemistry , biochemistry , biology , organic chemistry , genetics , polymer
A backbone‐caged sperm‐activating peptide (caged speract) that has a 2‐nitrobenzyl group at a backbone amide and a vastly reduced affinity for its receptor (IC 50 =950 nM) was synthesized. UV irradiation of caged speract photocleaves the 2‐nitrobenzyl group ( τ 1/2 =26 μs), restoring its affinity (IC 50 =0.67 nM) and ability to increase sperm intracellular pH and Ca 2+ , as intact speract. Backbone caging of the biological activity was more efficient than side chain caging, which adds a nitrobenzyl group on the peptide side chain. The backbone caging strategy described can be used as a general procedure to cage biologically active peptides, which have no side chain for introduction of a caging group.