Sequence Changes Modulate Peptoid Self-Association in Water
| Autor: | Ella K. Martinetto, Jonathan Huber, Kyra N. McComas, Jose L. Moreno, Amelia A. Fuller, Kalli M. Dowell, Alberto Ortega, Christian J. Jimenez, Anna L. Calkins |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Circular dichroism
Stereochemistry Peptidomimetic Sequence (biology) Peptide 02 engineering and technology 010402 general chemistry 01 natural sciences peptoid lcsh:Chemistry chemistry.chemical_compound Amphiphile Side chain Original Research chemistry.chemical_classification Peptoid size exclusion chromatography General Chemistry fluorescence spectroscopy 021001 nanoscience & nanotechnology peptidomimetic 0104 chemical sciences Chemistry chemistry lcsh:QD1-999 Helix circular dichroism (CD) spectroscopy 0210 nano-technology self-association |
| Zdroj: | Frontiers in Chemistry, Vol 8 (2020) Frontiers in Chemistry |
| ISSN: | 2296-2646 |
| DOI: | 10.3389/fchem.2020.00260/full |
| Popis: | Peptoids, N-substituted glycine oligomers, are a class of diverse and sequence-specific peptidomimetics with wide-ranging applications. Advancing the functional repertoire of peptoids to emulate native peptide and protein functions requires engineering peptoids that adopt regular secondary and tertiary structures. An understanding of how changes to peptoid sequence change structural features, particularly in water-soluble systems, is underdeveloped. To address this knowledge gap, five 15-residue water-soluble peptoids that include naphthalene-functionalized side chains were designed, prepared, and subjected to a structural study using a palette of techniques. Peptoid sequence designs were based on a putative amphiphilic helix peptoid bearing structure-promoting (S)-N-(1-naphthylethyl)glycine residues whose self-association in water has been studied previously. New peptoid variants reported here include sequence changes that influenced peptoid conformational flexibility, functional group patterning (amphiphilicity), and hydrophobicity. Peptoid structures were evaluated and compared using circular dichroism spectroscopy, fluorescence spectroscopy, and size exclusion chromatography. Spectral data confirmed that sequence changes alter peptoids' degree of assembly and the organization of self-assembled structures in aqueous solutions. Insights gained in these studies will inform the design of new water-soluble peptoids with regular structural features, including desirable higher-order (tertiary and quaternary) structural features. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|