Exploring structural features of folded peptide architectures in the construction of nanomaterials

Misra, Rajkumar; Reja, Rahi M.; Narendra, Lagumaddepalli V.; George, Gijo; Raghothama, Srinivasarao; Gopi, Hosahudya N.

doi:10.1039/c6cc04502b

Cited by 19 publications

(17 citation statements)

References 43 publications

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“…Therefore, unidirectional helices could be preferred in polar media due to their better electrostatic interactions with polar solvent molecules. This is confirmed by our recent results that demonstrated that 12/10‐helices lose their stability in polar solvents and are even transformed into unfolded structures by introducing aromatic α‐amino acids …”

Section: Theoretical Studiessupporting

confidence: 83%

Modulating the Structural Properties of α,γ‐Hybrid Peptides by α‐Amino Acid Residues: Uniform 12‐Helix Versus “Mixed” 12/10‐Helix

Misra

Kalpana

Hofmann³

et al. 2017

Chemistry A European J

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The most important natural α- and 3 -helices are stabilized by unidirectional intramolecular hydrogen bonds along the helical cylinder. In contrast, we report here on 12/10-helical conformations with alternately changing hydrogen-bond directionality in sequences of α,γ-hybrid peptides P1-P5 [P1: Boc-Ala-Aic-Ala-Aic-COOH; P2: Boc-Leu-Aic-Leu-Aic-OEt; P3: Boc-Leu-Aic-Leu-Aic-Leu-Aic-Aib-OMe; P4: Boc-Ala-Aic-Ala-Aic-Ala-Aic-Ala-OMe; P5: Boc-Leu-Aic-Leu-Aic-Leu-Aic-Leu-Aic-Aib-OMe; Aic=4-aminoisocaproic acid, Aib=2-aminoisobutyric acid] composed of natural α-amino acids and the achiral γ -dimethyl substituted γ-amino acid Aic in solution and in single crystals. The helical conformations are stabilized by alternating i→i+3 and i→i-1 intramolecular hydrogen bonds. The experimental data are supported by ab initio MO calculations. Surprisingly, replacing the natural α-amino acids of the sequence by the achiral dialkyl amino acid Ac c [P6: Boc-Ac c-Aic-Ac c-Aic-Ac c-Aic-Ac c-Aic-Ac c-CONHMe; Ac c = 1-aminocyclohexane-1-carboxylic acid] led to a 12-helix with unidirectional hydrogen bonds showing an entirely different backbone conformation. The results presented here emphasize the influence of the structure of the α-amino acid residues in dictating the helix types in α,γ-hybrid peptide foldamers and demonstrate the consequences for folding of small structural variations in the monomers.

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Section: Theoretical Studiessupporting

confidence: 83%

Modulating the Structural Properties of α,γ‐Hybrid Peptides by α‐Amino Acid Residues: Uniform 12‐Helix Versus “Mixed” 12/10‐Helix

Misra

Kalpana

Hofmann³

et al. 2017

Chemistry A European J

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“…Here, the hollowness of peptide nanoparticles of 6a (Boc-Phe-Phe- tz -A N(Boc) 2 ) allows encapsulation of CF. 23,31,32 The confocal images for 6a show that fluorescent molecules entered the cavity of spherical peptide nanoparticles (Figure 12A) upon incubation with CF. A similar experiment carried out with other tz peptides indicated subtle variations in their morphologies (Table 2).…”

Section: Resultsmentioning

confidence: 99%

Self-Assembly of Diphenylalanine–Peptide Nucleic Acid Conjugates

2019

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The synthesis and self-assembled nanostructures of a series of nucleopeptides (NPs) derived from the dipeptide Phe–Phe and the peptide nucleic acid unit which are covalently attached through an amide or a triazole linker are described. Depending on the variables such as protecting groups, linkers, and nucleobases, spherical nanoparticles were observed through scanning electron microscopy and high-resolution transmission electron microscopy images, and the porous nature of representative NPs was corroborated by carboxyfluorescein entrapment. Hydrophobic substituents on different sites of NPs and solvents employed for peptide self-assembly played a crucial role for corresponding morphologies. The stability of nanoparticles was also probed under external stimuli such as pH, temperature, and enzymatic hydrolysis using proteolytic enzymes. The semiconducting nature of the NP-modified carbon electrodes suggested their potential use as a new capacitor material.

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“…Thus, curcumin encapsulated GC1 vesicles in methanol (control sample) were incubated with (i) 5 eq of TBAF in 1:1 methanol:H 2 O; (ii) 12 eq of LD in 1:1 methanol:H 2 O; and (iii) 12 eq of LD in methanol for 24 h (see experimental section, ESI†) to study the release of curcumin . Fluorescence emission spectra showed enhancement in the fluorescence intensity of curcumin encapsulated GC1 with stimuli LD , when MeOH was the solvent (Figure ).…”

Section: Resultsmentioning

confidence: 99%

Solid‐Phase Synthesis of Clickable Psicofuranose Glycocarbamates and Application of Their Self‐Assembled Nanovesicles for Curcumin Encapsulation

et al. 2020

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Among the cyclic forms of carbohydrates, pyranoside derivatives have widely contributed to the well‐defined nanoassemblies. However, nanoassemblies originating from furanoside derivatives/oligomers, excluding nucleosides are underrepresented. Herein, we discuss the design and solid‐phase synthesis of homoligomers of a new class of clickable psicofuranose glycocarbamates that display nanovesicular/spherical nanostructures, an occurrence rarely observed in furanoside oligomers. The key intermediate, D‐(‐)‐fructose derived 2‐azido psicofuranose carbonate, was converted into dimeric and tetrameric azido‐glycocarbamates on solid‐phase which on subsequent “Click” reaction provided triazolyl glycocarbamates. These amphiphilic glycocarbamates self‐assembled into thermally and proteolytically stable spherical vesicles of 200‐800 nm size with visible hollow nature in CH3OH and tightly packed sphericals in CH3OH‐H2O. These nanostructures are characterized by various microscopy techniques. Effect of Cu+2 and Zn+2 ions, various cationic stimuli on the morphology of these nanostructures was studied. Hydrophobic drug curcumin was encapsulated in the hollow vesicles and release of the drug was investigated.

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Exploring structural features of folded peptide architectures in the construction of nanomaterials

Cited by 19 publications

References 43 publications

Modulating the Structural Properties of α,γ‐Hybrid Peptides by α‐Amino Acid Residues: Uniform 12‐Helix Versus “Mixed” 12/10‐Helix

Modulating the Structural Properties of α,γ‐Hybrid Peptides by α‐Amino Acid Residues: Uniform 12‐Helix Versus “Mixed” 12/10‐Helix

Self-Assembly of Diphenylalanine–Peptide Nucleic Acid Conjugates

Solid‐Phase Synthesis of Clickable Psicofuranose Glycocarbamates and Application of Their Self‐Assembled Nanovesicles for Curcumin Encapsulation

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