Small Caged Molecules Used to Control Protein Activity

Small Caged Molecules Used to Control Protein Activity 

and many others [138]. Because the synthesis and application of these small molecules has been thoroughly reviewed before [1, 7, 44, 139], we will not discuss them in detail. 

2 x 10-6 M) and gave instantaneous recovery of activity after irradiation (IC50 = 3.6 x 10-8 M, as for natural AIP). Interestingly, the photolysis byproduct nitrosobenzaldehyde did not interfere with the behavior of the photoactivated peptides. 

Interestingly, no differences in activity toward All receptors in human neuroblastoma SMS-KAN cells were found between caged and unmodified All peptides, indicating that the Tyr residue in this eight-amino acid peptide is not involved in binding to the receptor [142]. 

The 20-amino acid residue peptide RS-20, whose sequence derives from smooth muscle myosin light chain kinase (MLCK), is a well-known calmodulin binding peptide [144], Both, RS-20 and LMS-1, a 13-residue peptide derived from the autoinhibitory domain of MLCK, have the capability of inhibiting MLCK phosphorylation activity, normally directed toward the molecular motor, actin binding protein myosin II, which is involved in physiological phenomena like cell polarization and locomotion [145, 146]. 

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