Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Characteristic structural parameters for the γ-peptide 14-helix: importance of subunit preorganization.

Literature DB >> 21567680

Characteristic structural parameters for the γ-peptide 14-helix: importance of subunit preorganization.

Li Guo¹, Weicheng Zhang, Andrew G Reidenbach, Michael W Giuliano, Ilia A Guzei, Lara C Spencer, Samuel H Gellman.

Abstract

Entities: Chemical Species

Mesh：

Substances：

Year: 2011 PMID： 21567680 PMCID： PMC3429132 DOI： 10.1002/anie.201101301

Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN： 1433-7851 Impact factor: 15.336

× No keyword cloud information.

40 in total

Review 1. beta-Peptides: from structure to function.

Authors: R P Cheng; S H Gellman; W F DeGrado
Journal: Chem Rev Date: 2001-10 Impact factor: 60.622

2. Parallel sheet secondary structure in gamma-peptides.

Authors: M G Woll; J R Lai; I A Guzei; S J Taylor; M E Smith; S H Gellman
Journal: J Am Chem Soc Date: 2001-11-07 Impact factor: 15.419

3. De novo design, synthesis, and characterization of antimicrobial beta-peptides.

Authors: D Liu; W F DeGrado
Journal: J Am Chem Soc Date: 2001-08-08 Impact factor: 15.419

4. Helical beta-peptide inhibitors of the p53-hDM2 interaction.

Authors: Joshua A Kritzer; James D Lear; Michael E Hodsdon; Alanna Schepartz
Journal: J Am Chem Soc Date: 2004-08-11 Impact factor: 15.419

Review 5. Structural chemistry of peptides containing backbone expanded amino acid residues: conformational features of β, γ, and hybrid peptides.

Authors: Prema G Vasudev; Sunanda Chatterjee; Narayanaswamy Shamala; Padmanabhan Balaram
Journal: Chem Rev Date: 2010-09-15 Impact factor: 60.622

6. Helix geometry in proteins.

Authors: D J Barlow; J M Thornton
Journal: J Mol Biol Date: 1988-06-05 Impact factor: 5.469

7. Antifungal activity from 14-helical beta-peptides.

Authors: Amy J Karlsson; William C Pomerantz; Bernard Weisblum; Samuel H Gellman; Sean P Palecek
Journal: J Am Chem Soc Date: 2006-10-04 Impact factor: 15.419

8. Gamma2-, gamma3-, and gamma(2,3,4)-amino acids, coupling to gamma-hexapeptides: CD spectra, NMR solution and X-ray crystal structures of gamma-peptides.

Authors: Dieter Seebach; Meinrad Brenner; Magnus Rueping; Bernhard Jaun
Journal: Chemistry Date: 2002-02-02 Impact factor: 5.236

9. A new class of foldamers based on cis-gamma-amino-L-proline.

Authors: Josep Farrera-Sinfreu; Laura Zaccaro; David Vidal; Xavier Salvatella; Ernest Giralt; Miquel Pons; Fernando Albericio; Miriam Royo
Journal: J Am Chem Soc Date: 2004-05-19 Impact factor: 15.419

10. Structure-activity studies of 14-helical antimicrobial beta-peptides: probing the relationship between conformational stability and antimicrobial potency.

Authors: Tami L Raguse; Emilie A Porter; Bernard Weisblum; Samuel H Gellman
Journal: J Am Chem Soc Date: 2002-10-30 Impact factor: 15.419

5 in total

Characteristic structural parameters for the γ-peptide 14-helix: importance of subunit preorganization.

Review 1. beta-Peptides: from structure to function.

2. Parallel sheet secondary structure in gamma-peptides.

3. De novo design, synthesis, and characterization of antimicrobial beta-peptides.

4. Helical beta-peptide inhibitors of the p53-hDM2 interaction.

Review 5. Structural chemistry of peptides containing backbone expanded amino acid residues: conformational features of β, γ, and hybrid peptides.

6. Helix geometry in proteins.

7. Antifungal activity from 14-helical beta-peptides.

8. Gamma2-, gamma3-, and gamma(2,3,4)-amino acids, coupling to gamma-hexapeptides: CD spectra, NMR solution and X-ray crystal structures of gamma-peptides.

9. A new class of foldamers based on cis-gamma-amino-L-proline.

10. Structure-activity studies of 14-helical antimicrobial beta-peptides: probing the relationship between conformational stability and antimicrobial potency.

1. Heterogeneous H-bonding in a foldamer helix.

2. Impact of γ-Amino Acid Residue Preorganization on α/γ-Peptide Foldamer Helicity in Aqueous Solution.

3. Differential impact of β and γ residue preorganization on α/β/γ-peptide helix stability in water.

4. New preorganized γ-amino acids as foldamer building blocks.

5. Evaluation of a cyclopentane-based γ-amino acid for the ability to promote α/γ-peptide secondary structure.