These peptides exhibited different bioactivity potencies at 100 µg. The three novel peptides produced were named as CSP1 (FFRSKLLSDGAAAAKGALLPQYW), CSP2 (RCMAFLLSDGAAAAQQLLPQYW), and CSP3 (DPAQPNYPWTAVLVFRH). Thus, our system, including the diagram, is a promising tool for searching biological active molecules such as peptide-based drugs.Ĭumin seed-derived peptides were extracted, fractionated, and identified in this study. These results define a peptide library suitable for screening of intracellular functional peptides. We summarized our data in a scatter diagram that plots hydrophobicity versus isoelectric point (pI) of conjugated peptides. We found that the internalization ability of CPP-conjugated peptides varied greatly depending on the property of the conjugated peptides, and anionic peptides drastically decreased the uptake ability. By using this screening system, we determined how the cellular uptake properties of CPP-conjugated peptides varied depending on the properties of the conjugated peptides. Here, we demonstrate a novel peptide array system for screening intracellular functional peptides, in which both cell-penetrating peptide (CPP) domain and photo-cleavable linkers are used. An effective high-throughput screening system for intracellular functional peptides has not been reported. Therefore, the screening and design of intracellular functional peptides are more difficult than that of extracellular ones. However, hydrophilic materials like peptides are difficult for cells to internalize. Peptides, especially intracellular functional peptides that can play a particular role inside a cell, have attracted attention as promising materials to control cell fate.

Photolinker ii