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Conflicts of Interest The authors declare no conflicts of interest. Data Availability Statement The data of this study are available from the corresponding author upon reasonable request. References 1, , , et al., “Ultrafast Laser Processing of Materials: From Science to Industry,” Light, Science & Applications 5, no. 8 (2016): 16133. 2 and , “Femtosecond Laser Micromachining in Transparent Materials,” Nature Photonics 2, no. 4 (2008): 219–225.
Abstract Cyclic peptides exhibit advantages in binding protein targets with high affinity and competency in inhibiting protein-protein interactions. Cyclic peptide phage display with more than a billion variants is an invaluable tool in drug discovery. However, achieving efficient peptide cyclization on phages remains a challenge because of the limited availability of reaction sites, which also restrict scaffold diversity.
A facile strategy for the construction of a phage display cyclic peptide library for the selection of functional macrocycles† Cyclic peptides represent invaluable scaffolds in biological affinity, providing diverse collections for discovering functional molecules targeting challenging biological entities and protein–protein interactions.
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