Entire Encapsulation of Thymopentin by Extended Biphen[3]arene Carboxylate for Improving Plasma Stability
Peptide-based therapy is appealing in modern medicine owing to its high activity and excellent biocompatibility. Poor stability, leading to unacceptable bioavailability, severely constrains its clinical application. Here, we proposed a general supramolecular approach for improving the plasma resista...
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| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-01-01
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| Series: | Molecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1420-3049/30/2/314 |
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| Summary: | Peptide-based therapy is appealing in modern medicine owing to its high activity and excellent biocompatibility. Poor stability, leading to unacceptable bioavailability, severely constrains its clinical application. Here, we proposed a general supramolecular approach for improving the plasma resistance of a commercially available peptide agent, thymopentin. The <sup>1</sup>H NMR results indicated that the large-sized extended biphen[3]arene carboxylate (ExBP3C) can entirely encapsulate this peptide at its main chain with a binding stoichiometry of 1:1 and <i>K</i><sub>a</sub> value of (1.87 ± 0.15) × 10<sup>5</sup> M<sup>−1</sup>, which varied radically from recognizing specific amino acid residues by carboxylatopillar[5]arene (CP5A). Notably, host–guest complexation by ExBP3C could maintain 24.85% of the original thymopentin amount for 60 min in the presence of rat plasma, whereas free thymopentin, or co-dosed with CP5A and cucurbit[7]uril, underwent rapid degradation and became undetectable within just 30 min. In addition, cytotoxicity and hemolysis assays preliminary demonstrated that the employment of ExBP3C as a supplementary material was relatively nontoxic at a cellular level. |
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| ISSN: | 1420-3049 |