Nanoparticle Materials as Chemical and Biological Tools for Peptides and Proteins

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PART 1: NON-TECHNICAL SUMMARYProteins are extremely important biomolecules involved in practically every biological process. Although synthetic materials that bind peptides and proteins in aqueous environments are highly desirable, they are difficult to produce due to complexity of biological peptides. The research group of Professor Yan Zhao at Iowa State University develops novel antibody-mimicking polymeric nanoparticles for sequence-specific recognition of peptides. These materials are expected to enable numerous applications in chemistry and biology including identification of functional residues responsible for Alzheimer’s disease, regulation of enzymatic catalysis, and purification of peptides and proteins. The research trains student researchers into professional scientists by exposing them to a wide range of skills in biomaterials science, physical organic chemistry, supramolecular chemistry, and polymer chemistry.PART 2: TECHNICAL SUMMARYProteins are extremely important biomolecules involved in practically every biological process. Although synthetic materials that bind peptides and proteins in competitive aqueous environments have numerous applications in chemistry and biology, they are difficult to produce because of complexity of the guest, subtle structural differences among some amino acids, and difficulty in molecular recognition in water. This project, funded by the Biomaterials Program of the Division of Materials Research, supports Professor Yan Zhao of Iowa State University to develop antibody-mimicking polymeric nanoparticles for sequence-specific recognition of peptides. The materials are prepared through molecular imprinting within cross-linked surfactant micelles and can be tuned systematically in their molecular recognition. With abilities to distinguish closely related amino acid residues, they can be used to probe functional roles of specific sequences in a long peptide, as well as flexible loops catalytically relevant in an enzyme. By their strong and tunable binding for peptides, they enable facile purification of peptides and proteins from complex mixtures.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.