Peptide design. Helix–helix motifs in synthetic sequences

Banerjee, Arindam; Raghothama, Srinivasarao; Balaram, Padmanabhan

doi:10.1039/a700624a

Cited by 24 publications

(10 citation statements)

References 33 publications

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“…Hence, these tripeptides aggregated through intermolecular hydrogen bonds to form gels. Figure 8 demonstrates that solvent perturbation experiments [79,80] on peptide 3 exhibit significant downfield shifts of all NH groups upon the addition of (CD 3 ) 2 SO (1% to 12.5%) into aggregated gel (5 wt%) of the peptide 3 in C 6 D 6 . The d value changes of NH(1), NH(2) and NH(3) are 0.89, 0.57 and 0.76 respectively.…”

Section: H Nmr Studymentioning

confidence: 96%

Low Molecular Weight Organogelators from Self-assembling Synthetic Tripeptides With Coded Amino Acids: Morphological, Structural, Thermodynamic and Spectroscopic Investigations

Das

Manna

Drew

et al. 2006

Supramolecular Chemistry

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Section: H Nmr Studymentioning

confidence: 96%

Low Molecular Weight Organogelators from Self-assembling Synthetic Tripeptides With Coded Amino Acids: Morphological, Structural, Thermodynamic and Spectroscopic Investigations

Das

Manna

Drew

et al. 2006

Supramolecular Chemistry

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“…76 A detailed study of an analogue peptide BocMet-Ala-Leu-Aib-Val-Ala-Acp-Val-Ala-Leu-Aib-ValAla-Phe-OMe has provided evidence for a folded Ushaped arrangement of the two helices in an apolar solvent like chloroform. 105 The use of d-residues as potential helix breakers has been investigated in the sequences Boc-Val-Ala-Leu-Aib-Val-Ala-Leu- 107±110 In the case of short synthetic peptides the terminating residue has invariably been the achiral residue Aib, 111,112 whereas in proteins Gly is most frequently found. 113 In the case of the Figure 11 illustrates the relative orientation of two helical segments for four distinct stereochemical alternatives for the linking tripeptide segments.…”

Section: Design Of Helix±helix Motifsmentioning

confidence: 99%

Stereochemical Control of Peptide Folding

Kaul

Balaram

1999

Bioorganic & Medicinal Chemistry

153

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AbstractÐStereochemically constrained amino acid residues that strongly favour speci®c backbone conformations may be used to nucleate and stabilize speci®c secondary structures in designed peptides. An overview of the use of aa-dialkyl amino acids in stabilizing helical structures in synthetic peptides is presented, with an emphasis on work carried out in the authors laboratory. a-Aminoisobutyric acid (Aib) and related achiral homologs facilitate stable helix formation in oligopeptides as exempli®ed by a large number of crystal structure determinations in the solid state. The ability to design conformationally rigid helical modules has been exploited in attempts to design structurally well characterized helix-linker±helix, using potential nonhelical linking segments. bHairpin design has been approached by exploiting the tendency of`prime turns' to nucleate hairpin formation. The use of nucleating D Pro-Gly segments has resulted in the generation of several well characterized b-hairpin structures, including the crystallographic observation of b-hairpin in a synthetic apolar octapeptide. Extensions of this approach to three stranded b-sheets and larger structures containing multiple D Pro-Gly segments appear readily possible.

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“…It can be concluded that no intramolecular hydrogen bonding is present and that Cys NH and Val NH are involved in intermolecular hydrogen bonds. [22] It is also clear from concentration-dependent NMR studies that there is no change in the secondary structure for the cyclic peptide -only the aggregation state is changing upon dilution. This is because other resonances do not change significantly with dilution (see the Supporting Information, Figure S3) except for the amide NHs (Cys NH and Val NH), which are involved in intermolecular hydrogen bonding.…”

Section: Methodsmentioning

confidence: 99%

Macroporous Materials from Self‐Assembling Synthetic Cyclic Peptide‐Based Compounds and Deposition of Dipeptide‐Capped Gold Nanoparticles on the Surfaces

Guha

Banerjee

2009

Macro Chemistry & Physics

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Two cyclic peptides are separately self‐assembled, one on top of the other, utilizing non‐covalent interactions – mainly intermolecular hydrogen bonding – to form a one‐dimensional array. These one‐dimensional arrays are further self‐assembled to construct macroporous materials. This is shown from TEM, AFM and FE‐SEM analyses. These materials have been used for adsorption and desorption of nitrogen gas. Moreover, they can act as suitable templates for the deposition of dipeptide capped gold nanoparticles on the surfaces of macroporous structures.magnified image

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Peptide design. Helix–helix motifs in synthetic sequences

Cited by 24 publications

References 33 publications

Low Molecular Weight Organogelators from Self-assembling Synthetic Tripeptides With Coded Amino Acids: Morphological, Structural, Thermodynamic and Spectroscopic Investigations

Low Molecular Weight Organogelators from Self-assembling Synthetic Tripeptides With Coded Amino Acids: Morphological, Structural, Thermodynamic and Spectroscopic Investigations

Stereochemical Control of Peptide Folding

Macroporous Materials from Self‐Assembling Synthetic Cyclic Peptide‐Based Compounds and Deposition of Dipeptide‐Capped Gold Nanoparticles on the Surfaces

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