Publications by authors named "Maria Soledad Garre Hernandez"
The binding process of insulin to its transmembrane receptor entails a sophisticated interplay between two proteins, each possessing two binding sites. Given the difficulties associated with the use of insulin in the treatment of diabetes, despite its remarkable efficacy, there is interest in smaller and more stable compounds than the native hormone that would effectively activate the receptor. Our study adopts a strategy focused on synthesizing extensive combinatorial libraries of bipodal compounds consisting of two distinct peptides linked to a molecular scaffold.
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- Insulin helps control the energy balance in our bodies and works by binding to its receptors.
- Scientists created special insulin dimers (two connected molecules) that can either trigger or block these receptors.
- Some of these dimers worked better than regular insulin at activating the receptors, suggesting they could be useful for more targeted treatments.
Multi-orthogonal molecular scaffolds can be applied as core structures of bioactive compounds. Here, we prepared four tri-orthogonal scaffolds based on adamantane or proline skeletons. The scaffolds were used for the solid-phase synthesis of model insulin mimetics bearing two different peptides on the scaffolds.
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