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- W4254351688 abstract "Objectives: D-proline is an isomer of L-proline, naturally occurring amino acid. Apart from this, several proline homologs and analogs are available in nature. For instance, hydroxyproline one of proline analog plays a key role in collagen function. Inhibition of collagenase activity plays a significant role in protecting the unbalanced turnover of collagen, caused due to inflammation and photoaging of skin. This prompted us to carry out the study on proline and prolinamide isomers.Methods: These proline and prolinamide isomers were evaluated on the docking behavior of bacterial collagenase using PatchDock. In addition, molecular physicochemical, drug-likeness, absorption, distribution, metabolism and excretion (ADME) analysis, synthesis, and characterization of four prolinamide isomers were also carried out.Results: All the four synthesized prolinamide isomers showed >90% yield. The molecular physicochemical analysis revealed that proline and prolinamide isomers showed nil violation and complied well with the Lipinski’s rule of five. ADME analysis showed that prolinamide isomers predicated to have blood–brain barrier permeability. Docking studies revealed that D (S, R) prolinamide isomer showed the maximum atomic contact energy (−115.09 kcal/mol) with that of Clostridium histolyticum collagenase.Conclusion: Thus, the present study showed the potential of proline and prolinamide isomers as collagenase inhibitors." @default.
- W4254351688 created "2022-05-12" @default.
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- W4254351688 date "2019-01-07" @default.
- W4254351688 modified "2023-09-30" @default.
- W4254351688 title "SYNTHESIS, CHARACTERIZATION, AND MOLECULAR DOCKING ANALYSIS OF PROLINE (PYRROLIDINE 2-CARBOXYLIC ACID) AND PROLINAMIDE (PYRROLIDINE 2-CARBOXYLIC ACID AMIDE) ISOMERS AS BACTERIAL COLLAGENASE INHIBITORS" @default.
- W4254351688 doi "https://doi.org/10.22159/ajpcr.2018.v12i1.29894" @default.
- W4254351688 hasPublicationYear "2019" @default.
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