{'fraction_non_alphanumeric': 0.009977827050997782, 'fraction_numerical': 0.0011086474501108647, 'mean_word_length': 5.946153846153846, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Diketopiperazine receptors: a novel class of highly selective receptors for binding small peptides.

A novel class of receptors consisting of a rigid diketopiperazine backbone and peptidic side chains has been developed with the use of combinatorial chemistry. These diketopiperazine receptors interact with peptidic substrates with high specificity as shown in combinatorial on-bead assays. The central diketopiperazine moiety can be easily obtained from natural 4-hydroxyproline and serves as a rigidifying template for the peptidic modules which allow for structural as well as functional variations. Screenings of several dye-marked receptor prototypes against an encoded tripeptide library demonstrated not only the high binding specificities of the diketopiperazine receptors towards peptides but also revealed that small structural changes induce significant changes in their binding properties.