Structural and morphological diversity of self-assembled synthetic γ-amino acid containing peptides

Abstract

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 (P), Boc-Gpn-Aib-Leu-Aib-OMe (P) and Boc-Gpn-Aib-Tyr-Aib-OMe (P) 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 P-P and the salt-prompted mineralization studies of peptide P under ambient conditions are studied. All three reported peptides P-P form diverse supramolecular scaffolds in solid states through non-covalent interactions to attain higher order architectures.

Light induced construction of porous covalent organic polymeric networks for significant enhancement of CO2 gas sorption

“…41 Peptide-based bolaamphiphiles are a unique class of amphiphiles, which can self-assemble into different architectures through noncovalent interactions upon the inuence of external stimuli. [42][43][44][45] Upon incorporation of a diacetylene moiety into the peptide backbones, peptide functionalized diacetylene-based amphiphiles can self-assemble into an oriented fashion and form self-assembled nanostructures. Peptide-functionalized diphenylbutadiyne-based bolaamphiphiles can also be polymerized using topochemical polymerization if they are appropriately oriented.…”

Modulating Hydrogen Bonded Self-assembled Patterns and Morphological Features by a Change in Side Chain of Third Amino Acid of Synthetic γ- Amino Acid Based Tripeptides

“…Conformational modulation and self‐assembled diversity of short peptides have been recently gained a considerable attention due to its immense importance in understanding the folding and self‐assembly of biomolecules. Conformational modulations in short hybrid peptides have been achieved by using various unnatural amino acids as constituents, chirality and by changing the N‐ and C‐terminal groups . Here, our objectives are (i) to probe the conformational modulation of two short peptides with sequences Boc‐Gpn‐Aib‐Xaa‐OMe (where Gpn=gabapentin, Xaa=Leu(L) for 1 and Phe(F) for 2 ) which varied only at C‐terminal residue both in solid as well as solution states (Scheme ), (ii) to explore the structural effects of backbone and side chain propensities in self‐assemble diversity of γαα‐based peptides 1 and 2 and (iii) to study the role of C‐terminal amino acids in the formation of diverse supramolecular self‐assemble morphological features.…”

“…Conformational modulations in short hybrid peptides have been achieved by using various unnatural amino acids as constituents, chirality and by changing the N-and C-terminal groups. [32][33][34][35][36][37] Here, our objectives are (i) to probe the conformational modulation of two short peptides with sequences Boc-Gpn-Aib-Xaa-OMe (where Gpn = gabapentin, Xaa = Leu(L) for 1 and Phe(F) for 2) which varied only at C-terminal residue both in solid as well as solution states (Scheme 1), (ii) to explore the structural effects of backbone and side chain propensities in self-assemble diversity of gaa-based peptides 1 and 2 and (iii) to study the role of C-terminal amino acids in the formation of diverse supramolecular self-assemble morphological features. Development of selfassembled biomimetic materials using synthetic building blocks has vast importance in material science and bioorganic chemistry.…”

The Diverse World of Foldamers: Endless Possibilities of Self-Assembly

“…The Aib-containing mixed α/γ-tetrapeptides, Boc-Gpn-Aib-Xaa-Aib-OMe ( Figure 22 f), where Gpn is gabapentin—a constrained achiral γ-amino acid whose β carbon is tethered in a cyclohexyl ring—were also able to generate fibers in different conditions [ 256 ]. According to NMR and CD studies, these hybrid tetrapeptides adopted different double turn conformations in solution, which were also found in the crystal by XRD.…”