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A database of experimentally validated cell-penetrating peptides (CPPs). CPPsite 2.0 holds around 1850 peptide entries, which is nearly two times than the entries in the previous version. The updated data were curated from research papers and patents published in last three years. It was observed that most of the CPPs discovered/ tested, in last three years, have diverse chemical modifications (e.g. non-natural residues, linkers, lipid moieties, etc.). We have compiled this information on chemical modifications systematically in the updated version of the database. In order to understand the structure-function relationship of these peptides, we predicted tertiary structure of CPPs, possessing both modified and natural residues, using state-of-the-art techniques. CPPsite 2.0 also maintains information about model systems (in vitro/in vivo) used for CPP evaluation and different type of cargoes (e.g. nucleic acid, protein, nanoparticles, etc.) delivered by these peptides. In order to assist a wide range of users, we developed a user-friendly responsive website, with various tools, suitable for smartphone, tablet and desktop users.


A collection of therapeutically important peptides from different peptide databases/datasets. These peptides were curated and classified based on their major function, therapeutic property and sub-function. The current version holds 19192 unique experimentally validated therapeutic peptide sequences having length between 2 and 50 amino acids. It covers peptides having natural, non-natural and modified residues. These peptides were systematically grouped into 10 categories based on their major function or therapeutic property like 1099 anticancer, 10585 antimicrobial, 1642 drug delivery and 1698 antihypertensive peptides. Briefly, users can take advantage of SATPdb in following ways: users can (i) search a peptide of interest in 22 peptide databases/datasets at one go and therefore save time, (ii) browse peptides of SATPdb with similar physicochemical properties or secondary structure content, (iii) extract moonlighting peptides with desired functions and (iv) extract structural information of most of the peptides including peptides with non-natural residues which can be used for further structure-to-function analysis and docking studies.