Proteomimetics as protein-inspired scaffolds with defined tertiary folding patterns.

Area of Science:

• Biochemistry and Medicinal Chemistry
• Supramolecular Chemistry
• Materials Science

Background:

• Proteins offer diverse molecular shapes, sizes, and functions, inspiring the search for artificial protein mimetics.
• Previous efforts focused on small protein fragments and isolated secondary structures.
• Recent interest has grown in designing artificial molecules that mimic larger, complex protein tertiary folds.

Purpose of the Study:

• To define and discuss recent advances in the field of proteomimetics.
• To categorize different approaches to proteomimetic design.
• To outline current challenges in the development of proteomimetics.

Main Methods:

• Categorization of proteomimetics based on structural and compositional modifications.
• Review of recent scientific literature and advancements in the field.
• Analysis of strategies for altering protein topology and backbone composition.

Main Results:

• Proteomimetics are classified into three main categories: modified protein domains, altered polypeptide backbones, and entirely non-natural folded architectures.
• Significant progress has been made in designing molecules that mimic complex protein folds.
• The field is advancing towards creating artificial molecules with tailored properties.

Conclusions:

• Proteomimetics represent a promising area for developing molecules with novel and improved functions.
• Further research is needed to overcome challenges in designing and synthesizing complex proteomimetic structures.
• The field holds potential for applications in medicine, materials science, and beyond.