d/l-Hybrid peptides are an attractive class of
molecular modality because they are able to exhibit high proteolytic
stability and unique structural diversity which cannot be accessed
by those consisting of only proteinogenic l-amino acids.
Despite such an expectation, it has not been possible to devise de
novo d/l-hybrid peptides capable of disrupting the
function of a protein target(s) due to the lack of an effective method
that reliably constructs a highly diverse library and screens active
species. Here we report for the first time construction of a library
consisting of 1012 members of macrocyclic d/l-hybrid peptides containing five kinds of d-amino
acids and performance of the RaPID selection against human EGFR as
a showcase to uncover PPI (protein–protein interaction) inhibitors.
We report the frequency stabilization of a diode laser by applying the dichroic-atomic-vapor laser lock (DAVLL) method to a thin Rb vapor cell. A 1-mm-long Rb vapor cell is used to obtain a sub-Doppler spectrum that is required for frequency locking, which is easier than in the case of using a saturated absorption spectrometer. A 794-nm diode laser is tuned to the Rb D
1 line, and sub-Doppler signals are observed by introducing a pumping beam and a probe beam in a perpendicular direction. We obtain error signals by subtracting the signals of σ+ polarized beams from that of σ- polarized beams in the presence of a magnetic field and stabilized the 794 nm diode laser frequency without modulating laser parameters. The stability of the 794-nm diode laser is evaluated using other independently stabilized diode laser.
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