Tolerance of acyclic residues in the beta-peptide 12-helix: access to diverse side-chain arrays for biological applications.

Tolerance of acyclic residues in the beta-peptide 12-helix: access to diverse side-chain arrays for biological applications. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Tolerance of acyclic residues in the beta-peptide 12-helix: access to diverse side-chain arrays for biological applications. Abstract Text:

Paul R LePlae,John D Fisk,Emilie A Porter,Bernard Weisblum,Samuel H Gellman,

Oligomeric backbones with well-defined conformational propensities can serve as scaffolds for displaying sets of functional groups in specific three-dimensional arrangements. beta-Peptides are particularly interesting in this regard because several distinct secondary structures can be induced by appropriate choice of beta-amino acid substitution pattern.3 The beta-peptide 12-helix (defined by 12-membered ring C=O(i)- -H-N(i + 3) hydrogen bonds) is of particular interest because this helix resembles the alpha-helix. To date 12-helices have been observed in beta-peptides comprised exclusively of residues containing a five-membered ring constraint. Here we show that 12-helical propensity is maintained when some cyclic beta-amino acid residues are replaced with more flexible acyclic residues. This result is important because use of acyclic residues greatly facilitates introduction of diverse side chains at specific sites along the 12-helix. We demonstrate the utility of this advance in the context of antibiotic design.

Tolerance of acyclic residues in the beta-peptide 12-helix: access to diverse side-chain arrays for biological applications. Publishing Authors By Initials

PR LePlae,JD Fisk,EA Porter,B Weisblum,SH Gellman,

For similar heterocyclic compounds: heterocyclic compounds, 1-ring: pyrrolidines research abstracts see: heterocyclic compounds: heterocyclic compounds, 1-ring: pyrrolidines research

PUBMED ID PMID:

MEDLINE DATE:

Tolerance of acyclic residues in the beta-peptide 12-helix: access to diverse side-chain arrays for biological applications. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of the American Chemical Society

VOLUME: 124

Page Numbers: 6820-1

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 19

MONTH: Jun

YEAR: 2002

Tolerance of acyclic residues in the beta-peptide 12-helix: access to diverse side-chain arrays for biological applications. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7503056

Tolerance of acyclic residues in the beta-peptide 12-helix: access to diverse side-chain arrays for biological applications. Keywords Mesh Terms:

KEYWORDS: Pyrrolidines

MESH TERMS: chemistry

Chemical & Substance for Abstract: Tolerance of acyclic residues in the beta-peptide 12-helix: access to diverse side-chain arrays for biological applications. Information

Substance Name: Lysine

Registry Number: 56-87-1

Grant and Affiliation Information for Tolerance of acyclic residues in the beta-peptide 12-helix: access to diverse side-chain arrays for biological applications.

AFFILIATION: Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

Country: United States

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Am Chem Soc

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Tolerance of acyclic residues in the beta-peptide 12-helix: access to diverse side-chain arrays for biological applications Related Publications

• (alpha/beta+alpha)-peptide antagonists of BH3 domain/Bcl-x(L) recognition: toward general strategies for foldamer-based inhibition of protein-protein interactions.
• An antiparallel alpha-helical coiled-coil model system for rapid assessment of side-chain recognition at the hydrophobic interface.
• Backbone thioester exchange: a new approach to evaluating higher order structural stability in polypeptides.
• Chimeric (alpha/beta + alpha)-peptide ligands for the BH3-recognition cleft of Bcl-XL: critical role of the molecular scaffold in protein surface recognition.
• Crystallographic characterization of the alpha/beta-peptide 14/15-helix.
• Discrete heterogeneous quaternary structure formed by alpha/beta-peptide foldamers and alpha-peptides.
• Effect of certain detergents on sewage treatment.
• Effects of conformational stability and geometry of guanidinium display on cell entry by beta-peptides.
• Enantioselective organocatalytic Michael additions of aldehydes to enones with imidazolidinones: cocatalyst effects and evidence for an enamine intermediate.
• Enantioselective organocatalytic aminomethylation of aldehydes: a role for ionic interactions and efficient access to beta2-amino acids.
• Environment-independent 14-helix formation in short beta-peptides: striking a balance between shape control and functional diversity.
• Exploration of backbone space in foldamers containing alpha- and beta-amino acid residues: developing protease-resistant oligomers that bind tightly to the BH3-recognition cleft of Bcl-xL.
• HeLa cell entry by guanidinium-rich beta-peptides: importance of specific cation-cell surface interactions.
• Hydrophobic core repacking in a coiled-coil dimer via phage display: insights into plasticity and specificity at a protein-protein interface.
• Interplay among folding, sequence, and lipophilicity in the antibacterial and hemolytic activities of alpha/beta-peptides.
• Mimicry of antimicrobial host-defense peptides by random copolymers.
• Origins of the high 14-helix propensity of cyclohexyl-rigidified residues in beta-peptides.
• Practical synthesis of enantiomerically pure beta2-amino acids via proline-catalyzed diastereoselective aminomethylation of aldehydes.
• Preferred side-chain constellations at antiparallel coiled-coil interfaces.
• Residue requirements for helical folding in short alpha/beta-peptides: crystallographic characterization of the 11-helix in an optimized sequence.
• Roles of salt and conformation in the biological and physicochemical behavior of protegrin-1 and designed analogues: correlation of antimicrobial, hemolytic, and lipid bilayer-perturbing activities.
• Secondary structural preferences of 2,2-disubstituted pyrrolidine-4-carboxylic acid oligomers: beta-peptide foldamers that cannot form internal hydrogen bonds.
• Stabilizing and destabilizing effects of phenylalanine --> F5-phenylalanine mutations on the folding of a small protein.
• Structure-activity studies of 14-helical antimicrobial beta-peptides: probing the relationship between conformational stability and antimicrobial potency.
• Targeting protein-protein interactions: lessons from p53/MDM2.
• Thermodynamic analysis of autonomous parallel beta-sheet formation in water.
• Thermodynamic analysis of beta-sheet secondary structure by backbone thioester exchange.
• Tolerance of acyclic residues in the beta-peptide 12-helix: access to diverse side-chain arrays for biological applications.
• Translocation of a beta-peptide across cell membranes.
• Unexpected relationships between structure and function in alpha,beta-peptides: antimicrobial foldamers with heterogeneous backbones.