RUI: peptide quasiracemates

The National Science Foundation Division of Materials Research awarded Whitworth University $404,800 on August 1, 2026, under the Mathematical and Physical Sciences program (CFDA 47.049) to study how molecular shape governs the organization of peptides in molecular crystals.

Dr. Kraig Wheeler leads research into racemic and quasiracemic peptide arrays, developing families of dipeptides and extended oligopeptides to understand how paired peptides form predictable structural patterns. The work aims to establish molecular shape as a design tool for crystal construction, with applications in biotechnology and materials science. The research contributes fundamental principles of molecular organization that inform the design and construction of new materials with potential societal impacts.

The project supports hands-on research training for undergraduate and high school students at Whitworth University, a predominantly undergraduate institution in Spokane, Washington. Outreach includes access to Whitworth's Crystallography Center, which serves a consortium of students and faculty from small colleges and universities across the greater academic community.

Performance of work occurs in Spokane, Washington, with a period of performance running from August 1, 2026, through July 31, 2029. This is a project grant funded through the Solid State and Materials Chemistry Program and the Biomaterials Program within the NSF Materials Research Section.

Abstract

Non-technical abstract: with support from the solid state and materials chemistry program and the biomaterials program in NSF?S materials research section a, DR. Kraig wheeler of whitworth university in spokane, washington, is studying how the shapes of small BIO-inspired molecules influence their organization in molecular crystals. This work develops families of small peptides, which are short chains of amino acids and the building blocks of proteins. When peptides are paired they form predictable patterns with outcomes that will contribute to the current understanding of the fundamental principles responsible for molecular organization. Because the use of molecular shape as a design tool for constructing crystals is rare but recognized as an important factor in determining crystal component alignment, the structural patterns derived from these research samples provide critical insight to the scientific community for the design and construction of materials with a variety of societal impacts, for example through applications in biotechnology. This project supports the training of a cohort of undergraduate and high school students through hands-on research experiences at whitworth university, a predominantly undergraduate institution. Outreach efforts from this program also include the use of whitworth?S crystallography center, which is open to a consortium of students and faculty from the greater academic community of small colleges and universities that support rigorous undergraduate programs. Technical abstract: this study examines how molecular shape governs molecular recognition, using racemic and quasiracemic approaches to construct engineered oligopeptide arrays. With support from the solid state and materials chemistry program and the biomaterials program in NSF?S materials research section a, the project explores the intricate topological relationships among families of dipeptides (acyclic and cyclic), extended peptides, and the predictable molecular arrays that form when coformer molecules are introduced into these systems. Because small changes to the molecular framework and pendant functional groups can produce drastically different modes of self-assembly, systematically varying molecular shape offers important opportunities to understand how key structural features drive the assembly behavior of each racemic or quasiracemic phase. The research team is using various experimental techniques ? Solid-phase peptide synthesis, X-RAY crystallography, and hot-stage thermomicroscopy ? And computational methods to systematically map the shape space of these materials and understand the role of topological features in the assembly of peptidic components. This strategy allows the research team to gather new insights into the molecular recognition profiles of oligopeptides, leading to the discovery of new materials controlled by the complementary topological features of the components which may lead to advances in biotechnology. At the same time the project provides a valuable platform to train the next generation of stem workforce. 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.- subawards are not planned for this award.