An Approach to Using X-Ray Crystallography to Understand Peptidomimetics

Researcher Information

Abstract

Peptidomimetics can fold into a variety of well-defined shapes. The goal of this project is to understand shape selection in a beta peptide foldamer with an alpha amino acid cap. This research represents interdisciplinary collaboration between KAIST, a research university in South Korea, and NSU. We solved the single crystal x-ray structure and found that the crystals of this molecule were orthorhombic in P21212with unit cell dimensions a=22.655(6), b=30.008(8), c=18.271(5) and a unit cell volume of 12421.2 Å3 (Z=8). We observed a total of 6 intermolecular hydrogen bonds within the beta peptide foldamer. Each of these hydrogen bonds make 12-membered rings within the structure, even including the alpha amino acid cap. These hydrogen bonds create a helical shape as they pull the ith carbonyl oxygen and the i + 3rd amid hydrogen together. This research demonstrates that it is possible to add a highly soluble alpha amino acid cap without changing the secondary structure of the beta peptidomimetic.

Faculty Sponsors

Dr. Russell Driver

Project Type

Event

Location

Alvin Sherman Library

Start Date

4-3-2024 12:30 PM

End Date

4-4-2024 1:30 PM

This document is currently not available here.

Share

COinS
 
Apr 3rd, 12:30 PM Apr 4th, 1:30 PM

An Approach to Using X-Ray Crystallography to Understand Peptidomimetics

Alvin Sherman Library

Peptidomimetics can fold into a variety of well-defined shapes. The goal of this project is to understand shape selection in a beta peptide foldamer with an alpha amino acid cap. This research represents interdisciplinary collaboration between KAIST, a research university in South Korea, and NSU. We solved the single crystal x-ray structure and found that the crystals of this molecule were orthorhombic in P21212with unit cell dimensions a=22.655(6), b=30.008(8), c=18.271(5) and a unit cell volume of 12421.2 Å3 (Z=8). We observed a total of 6 intermolecular hydrogen bonds within the beta peptide foldamer. Each of these hydrogen bonds make 12-membered rings within the structure, even including the alpha amino acid cap. These hydrogen bonds create a helical shape as they pull the ith carbonyl oxygen and the i + 3rd amid hydrogen together. This research demonstrates that it is possible to add a highly soluble alpha amino acid cap without changing the secondary structure of the beta peptidomimetic.