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

Bidragets oversatte titel: a-Peptide/ß-Peptoid Chimeras

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

78 Citationer (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.

Bidragets oversatte titel	a-Peptide/ß-Peptoid Chimeras
Originalsprog	Engelsk
Tidsskrift	Organic Letters
Vol/bind	9
Udgave nummer	8
Sider (fra-til)	1549–1552
Antal sider	4
ISSN	1523-7060
DOI	https://doi.org/10.1021/ol070316c
Status	Udgivet - 2007

Emneord

Det tidligere Farmaceutiske Fakultet

Adgang til dokumentet

10.1021/ol070316c

Citationsformater

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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",

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volume = "9",

pages = "1549–1552",

journal = "Organic Letters",

issn = "1523-7060",

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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 -