The design of biomimetic crystal modifiers is a versatile tool for controlling crystal habit. Our work focuses on the design and screening of peptides as growth inhibitors of calcium oxalate monohydrate (COM), a common constituent of human kidney stones. We will describe our results on the design of a small library of peptides containing alanine and aspartic acid amino acids arranged in varying sequences that mimic ubiquitous motifs in natural calcium-binding proteins. We have used a high-throughput approach to synthesize and screen peptide libraries as a quick and reliable assay to measure their efficacy for inhibiting COM crystallization. Our results show that subtle variations in amino acid sequences have a profound effect on growth inhibition, and the specificity for peptide binding to different COM crystal surfaces. This work establishes new paradigms in crystal inhibitor design with the potential to impact a variety of fields including drug discovery and advanced materials.

Design of biomimetic peptides as inhibitors of calcium oxalate monohydrate crystallization

245th National Meeting (2013)

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