AI Article Synopsis
- Human serum albumin (HSA) can enhance the effectiveness of short-lived drugs by extending their presence in the bloodstream when therapeutic agents are conjugated with albumin-binding moieties (ABMs).
- A new method was developed to prepare both HSA domain III and its d-enantiomer, allowing for structural and functional analyses that confirmed their mirror-image properties and ability to be recognized by the neonatal Fc receptor (FcRn).
- The synthetic l-HSA domain III showed similar binding characteristics to the native HSA site II, making the synthetic d-HSA domain III a valuable resource for studying how HSA recognizes molecules at that site.
Article Abstract
Human serum albumin (HSA) as a drug carrier can significantly improve the pharmacokinetic profiles of short-lived therapeutics. Conjugation of albumin-binding moieties (ABMs) to therapeutic agents may prolong their serum half-life by promoting their association with endogenous HSA. To discover a new molecular class of ABMs from mirror-image chemical space, a preparation protocol for bioactive HSA domain III and its d-enantiomer (d-HSA domain III) was established. Structural and functional analyses suggested that the synthetic protein enantiomers exhibited mirror-image structures and stereoselective neonatal fragement crystallizable receptor (FcRn) recognition. Additionally, the ligand-binding properties of synthetic l-HSA domain III were comparable with those of site II in native HSA, as confirmed using site II-selective fluorescent probes and an esterase substrate. Synthetic d-HSA domain III is an attractive tool for analyzing the site II-dependent molecular recognition properties of HSA.
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| http://dx.doi.org/10.1021/acs.bioconjchem.4c00150 | DOI Listing |
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