ChemInform Abstract: Controlling Peptide Structure

Wysong, C. L.; Yokum, T. S.; McLaughlin, Mark L.; Hammer, Robert P.

doi:10.1002/chin.199739344

Cited by 2 publications

(2 citation statements)

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“…29 This secondary structure was expected to be of marginal stability when compared with the a-helix, under these experimental conditions, due to the unfavorable hydration of its carbonyl groups which are not oriented enough away from the helix axis. After several, only partially successful, attempts from our 30 and other [31][32][33][34][35][36] groups, we synthesized three terminally blocked heptapeptides, each containing (i) two residues of ATANP, 2-amino-3-[1-(1,4,7-triazacyclononane)]-L-propanoic acid (see Fig. 1), a chiral C a -trisubstituted a-amino acid with excellent water-solubilizing properties and (ii) five residues of C atetrasubstituted a-amino acids, either the achiral Aib or the chiral L-Iva (isovaline; Fig.…”

Section: Electronic Spectroscopy (Ecd)mentioning

confidence: 94%

Electronic and vibrational signatures of peptide helical structures: A tribute to Anton Mario Tamburro

Formaggio¹,

Toniolo²

2010

Chirality

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Our efforts on the synthesis of peptides with well-characterized secondary structures, combined with detailed spectroscopic investigations, most of them performed in collaboration with internationally recognized experts, have allowed us to publish the electronic (electronic circular dichroism) and vibrational (FTIR absorption, vibrational circular dichroism, Raman, and Raman optical activity) signatures of the poorly studied peptide 3(10)-helix (and the related β-bend ribbon spiral conformation as well) in comparison with those already known for the classical α-helix.

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Section: Electronic Spectroscopy (Ecd)mentioning

confidence: 94%

Electronic and vibrational signatures of peptide helical structures: A tribute to Anton Mario Tamburro

Formaggio¹,

Toniolo²

2010

Chirality

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“…In addition to the antimicrobial nature of amphipathic, α‐helical peptides, there have also been reports of short, amphipathic, 3 10 ‐helical peptides that exhibit antibacterial activity (21,28). As 3 10 ‐helical peptides (rise of 1.94 Å per amino acid; 34) are about 20% longer than α‐helical peptides (rise of 1.5 Å per amino acid; 30) with the same number of residues, we hypothesized that amphipathic, 3 10 ‐helical peptides might retain biologic activity at shorter peptide lengths (e.g. 9‐mer) than analogous α‐helical peptides.…”

Section: Introductionmentioning

confidence: 99%

Improved solid‐phase synthesis of α,α‐dialkylated amino acid‐rich peptides with antimicrobial activity*

Haynes

Hagins

Juban

et al. 2005

The Journal of Peptide Research

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A homologous series of nonapeptides and their acetylated versions were successfully prepared using solid-phase synthetic techniques. Each nonapeptide was rich in alpha,alpha-dialkylated amino acids [one 4-aminopiperidine-4-carboxylic acid (Api) and six alpha-aminoisobutyric acid (Aib) residues] and also included lysines or lysine analogs (two residues). The incorporation of the protected dipeptide 9-fluorenylmethyloxycarbonyl (Fmoc)-Aib-Aib-OH improved the purity and overall yields of these de novo designed peptides. The helix preference of each nonapeptide was investigated in six different solvent environments, and each peptide's antimicrobial activity and cytotoxicity were studied. The 3(10)-helical, amphipathic design of these peptides was born out most prominently in the N-terminally acetylated peptides. Most of the peptides exhibited modest activity against Escherichia coli and no activity against Staphylococcus aureus. The nonacetylated peptides (concentrations < or =100 microM) and the acetylated peptides (concentrations < or = 200 microM) did not exhibit any significant cytotoxicity with normal (nonactivated) murine macrophages.

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ChemInform Abstract: Controlling Peptide Structure

Cited by 2 publications

References 0 publications

Electronic and vibrational signatures of peptide helical structures: A tribute to Anton Mario Tamburro

Electronic and vibrational signatures of peptide helical structures: A tribute to Anton Mario Tamburro

Improved solid‐phase synthesis of α,α‐dialkylated amino acid‐rich peptides with antimicrobial activity*

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