Structural and morphological diversity of self-assembled synthetic γ-amino acid containing peptides
| Autor: | Brice Kauffmann, Maruthi Konda, Dnyaneshwar B. Rasale, Apurba K. Das |
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| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular Cyclohexanecarboxylic Acids Surface Properties Stereochemistry Supramolecular chemistry Peptide Crystallography X-Ray 010402 general chemistry 01 natural sciences Biochemistry Self assembled Turn (biochemistry) Amines Amino Acids Particle Size Physical and Theoretical Chemistry gamma-Aminobutyric Acid chemistry.chemical_classification Molecular Structure 010405 organic chemistry Organic Chemistry Hydrogen Bonding Combinatorial chemistry 0104 chemical sciences Amino acid Solvent chemistry Titration Gabapentin Oligopeptides |
| Zdroj: | Organic & Biomolecular Chemistry. 14:4089-4102 |
| ISSN: | 1477-0539 1477-0520 |
| Popis: | Regulating the nanostructural morphology of synthetic hybrid peptides through external stimuli is still a great challenge. Here, we report the synthesis of constrained amino acid building block gabapentin (Gpn) based hybrid peptides and their structural and morphological diversity in different conditions. The synthesized three hybrid peptides Boc-Gpn-Aib-Phe-Aib-OMe (P1), Boc-Gpn-Aib-Leu-Aib-OMe (P2) and Boc-Gpn-Aib-Tyr-Aib-OMe (P3) are folded into C12/C10 hydrogen-bonded double turn conformations. The double turn feature is probed and confirmed by conformational analysis of hybrid peptides using 2D-NMR studies and X-ray crystallography. DMSO-d6 solvent titration investigations also support the double turn conformation adopted by our reported peptides in CDCl3 solution. Solvent assisted self-assembled morphological features of peptides P1–P3 and the salt-prompted mineralization studies of peptide P1 under ambient conditions are studied. All three reported peptides P1–P3 form diverse supramolecular scaffolds in solid states through non-covalent interactions to attain higher order architectures. |
| Databáze: | OpenAIRE |
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