α-Peptide/ß-Peptoid Chimeras

Christian Adam Olsen; Gitte  Bonke; Line Vedel; Anne Adsersen; Matthias Witt; Henrik Franzyk; Jerzy W. Jaroszewski

doi:10.1021/ol070316c

α-Peptide/ß-Peptoid Chimeras

Christian Adam Olsen, Gitte Bonke, Line Vedel, Anne Adsersen, Matthias Witt, Henrik Franzyk, Jerzy W. Jaroszewski

78 Citations (Scopus)

Abstract

We describe the synthesis and characterization of the first generation of oligomers consisting of alternating repeats of a-amino acids and chiral N-alkyl-ß-alanine (ß-peptoid) residues. These chimeras are stable toward proteolysis, non-hemolytic, and possess antibacterial activity comparable to well-known antimicrobial agents. Moreover, the chimeras exhibit length-dependent, concentration-dependent, solvent-dependent, and ion-strength-dependent ellipticity, indicating the presence of a secondary structure in solution. Thus, a-peptide/ß-peptoid oligomers represent a promising novel peptidomimetic backbone construct for biologically active ligands.

Translated title of the contribution	a-Peptide/ß-Peptoid Chimeras
Original language	English
Journal	Organic Letters
Volume	9
Issue number	8
Pages (from-to)	1549–1552
Number of pages	4
ISSN	1523-7060
DOIs	https://doi.org/10.1021/ol070316c
Publication status	Published - 2007

Keywords

Former Faculty of Pharmaceutical Sciences

Access to Document

10.1021/ol070316c

Cite this

@article{8c1965c0ca6311dcbee902004c4f4f50,

title = "α-Peptide/{\ss}-Peptoid Chimeras",

abstract = "We describe the synthesis and characterization of the first generation of oligomers consisting of alternating repeats of a-amino acids and chiral N-alkyl-{\ss}-alanine ({\ss}-peptoid) residues. These chimeras are stable toward proteolysis, non-hemolytic, and possess antibacterial activity comparable to well-known antimicrobial agents. Moreover, the chimeras exhibit length-dependent, concentration-dependent, solvent-dependent, and ion-strength-dependent ellipticity, indicating the presence of a secondary structure in solution. Thus, a-peptide/{\ss}-peptoid oligomers represent a promising novel peptidomimetic backbone construct for biologically active ligands.",

keywords = "Former Faculty of Pharmaceutical Sciences",

author = "Olsen, {Christian Adam} and Gitte Bonke and Line Vedel and Anne Adsersen and Matthias Witt and Henrik Franzyk and Jaroszewski, {Jerzy W.}",

year = "2007",

doi = "10.1021/ol070316c",

language = "English",

volume = "9",

pages = "1549–1552",

journal = "Organic Letters",

issn = "1523-7060",

publisher = "American Chemical Society",

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TY - JOUR

T1 - α-Peptide/ß-Peptoid Chimeras

AU - Olsen, Christian Adam

AU - Bonke, Gitte

AU - Vedel, Line

AU - Adsersen, Anne

AU - Witt, Matthias

AU - Franzyk, Henrik

AU - Jaroszewski, Jerzy W.

PY - 2007

Y1 - 2007

N2 - We describe the synthesis and characterization of the first generation of oligomers consisting of alternating repeats of a-amino acids and chiral N-alkyl-ß-alanine (ß-peptoid) residues. These chimeras are stable toward proteolysis, non-hemolytic, and possess antibacterial activity comparable to well-known antimicrobial agents. Moreover, the chimeras exhibit length-dependent, concentration-dependent, solvent-dependent, and ion-strength-dependent ellipticity, indicating the presence of a secondary structure in solution. Thus, a-peptide/ß-peptoid oligomers represent a promising novel peptidomimetic backbone construct for biologically active ligands.

AB - We describe the synthesis and characterization of the first generation of oligomers consisting of alternating repeats of a-amino acids and chiral N-alkyl-ß-alanine (ß-peptoid) residues. These chimeras are stable toward proteolysis, non-hemolytic, and possess antibacterial activity comparable to well-known antimicrobial agents. Moreover, the chimeras exhibit length-dependent, concentration-dependent, solvent-dependent, and ion-strength-dependent ellipticity, indicating the presence of a secondary structure in solution. Thus, a-peptide/ß-peptoid oligomers represent a promising novel peptidomimetic backbone construct for biologically active ligands.

KW - Former Faculty of Pharmaceutical Sciences

U2 - 10.1021/ol070316c

DO - 10.1021/ol070316c

M3 - Journal article

SN - 1523-7060

VL - 9

SP - 1549

EP - 1552

JO - Organic Letters

JF - Organic Letters

IS - 8

ER -