X-Ray Crystallography of Self-Assembling Materials

Abstract

This research represents an interdisciplinary collaboration between NSU and KAIST, a leading research university in South Korea, and involves organic synthesis, X-ray crystallography, and materials selfassembly. This research informs the design of a new generation of self-assembling materials with improved physical properties for biomedical and technological applications.

Through analysis of the software packages CRYSTALS and Mercury, the structure of the molecule was found. The X-ray crystal’s parameters were found to be triclinic in P1 with a = 8.7008(5), b = 11.5507(7), c = 12.8580(8), a = 69.8418(18), b = 80.9295(18), g = 88.4199(18) and a unit cell volume of 1197.41(7) Å3 (Z = 1). The helical structure of the peptide backbone is interrupted by solvent intercalation. This structure is interesting because it has a disordered solvent pocket and a helical peptide backbone. The forces that hold the crystal together give us a clue as to why these can self-assemble into vehicles for active pharmaceutical ingredient delivery.

Faculty Sponsors

Dr. Russell Driver

Project Type

Event

Location

Alvin Sherman Library

Start Date

4-5-2023 12:00 PM

End Date

4-6-2023 4:00 PM

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Apr 5th, 12:00 PM Apr 6th, 4:00 PM

X-Ray Crystallography of Self-Assembling Materials

Alvin Sherman Library

This research represents an interdisciplinary collaboration between NSU and KAIST, a leading research university in South Korea, and involves organic synthesis, X-ray crystallography, and materials selfassembly. This research informs the design of a new generation of self-assembling materials with improved physical properties for biomedical and technological applications.

Through analysis of the software packages CRYSTALS and Mercury, the structure of the molecule was found. The X-ray crystal’s parameters were found to be triclinic in P1 with a = 8.7008(5), b = 11.5507(7), c = 12.8580(8), a = 69.8418(18), b = 80.9295(18), g = 88.4199(18) and a unit cell volume of 1197.41(7) Å3 (Z = 1). The helical structure of the peptide backbone is interrupted by solvent intercalation. This structure is interesting because it has a disordered solvent pocket and a helical peptide backbone. The forces that hold the crystal together give us a clue as to why these can self-assemble into vehicles for active pharmaceutical ingredient delivery.