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Synthesis and circular dichroism spectroscopic investigations of oligomeric β-peptoids with α-chiral side chains
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry, Organic Chemistry I.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry, Organic Chemistry I.
2006 (English)In: Organic Letters, ISSN 1523-7060, E-ISSN 1523-7052, Vol. 8, no 20, 4533-4536 p.Article in journal (Refereed) Published
Abstract [en]

Biomimetic oligomers are of large interest both as targets for combinatorial and parallel synthetic efforts and as foldamers. For example, shorter peptoid derivatives of beta-peptides, i.e., oligo-N-substituted beta-Ala, have been described as potential lead structures. Herein, we describe a solid-phase synthetic route to beta-peptoids with alpha-chiral aromatic N-substituents up to 11 residues long. Furthermore, the folding propensities of these oligomers were investigated by circular dichroism (CD) spectroscopy.

Place, publisher, year, edition, pages
2006. Vol. 8, no 20, 4533-4536 p.
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-95284DOI: 10.1021/ol061717fISI: 000240654700038PubMedID: 16986943OAI: oai:DiVA.org:uu-95284DiVA: diva2:169443
Available from: 2006-12-22 Created: 2006-12-22 Last updated: 2017-12-14Bibliographically approved
In thesis
1. Conformational Stability!?: Synthesis and Conformational Studies of Unnatural Backbone Modified Peptides
Open this publication in new window or tab >>Conformational Stability!?: Synthesis and Conformational Studies of Unnatural Backbone Modified Peptides
2006 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The beauty of the wide functionality of proteins and peptides in Nature is determined by their ability to adopt three-dimensional structures. This thesis describes artificial molecules developed to mimic secondary structures similar to those found crucial for biological activities.

In the first part of this thesis, we focused on post-translational modifications of a class of unnatural oligomers known as β-peptides. Through the design and synthesis of a glycosylated β3-peptide, the first such hybrid conjugate was reported. In this first report, a rather unstable 314-helical structure was found. Subsequently, a collection of six new glycosylated β3-peptides was synthesized with the aim to optimize the helical stability in water.

The ability of natural proteins, i.e. lectins, to recognize the carbohydrate residue on these unnatural peptide backbones was investigated through a biomolecular recognition study.

The second part of this thesis concerns the design of conformationally homogeneous scaffolds, which could be of importance for biomedical applications. In paper V, four- and five-membered cyclic all-β3-peptides were investigated for this purpose. In a subsequent paper, a completely different strategy was employed; herein, the ability of a single β2-amino acid to restrict the conformational freedom of a cyclic α-peptide was studied.

In the third part of this thesis, we synthesized and investigated the folding propensities of novel backbone modified oligomers, i.e. β-peptoids (N-substituted β-Ala) with α-chiral side chains.

The collective results of these studies have established the procedures required for synthesis of glycosylated β-peptides and deepened our understanding of the factors governing folding among such oligomers. Moreover, it was established that β-amino acids can be a useful tool to increase conformational stability of cyclic peptides.

Place, publisher, year, edition, pages
Uppsala: Acta Universitatis Upsaliensis, 2006. 78 p.
Series
Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, ISSN 1651-6214 ; 253
Keyword
Organic chemistry, Conformational investigations, β-peptides, glycosylation, biomolecular recognition, cyclic β³-peptides, cyclic mixed α/β²-peptides, β-peptoids, Organisk kemi
Identifiers
urn:nbn:se:uu:diva-7420 (URN)91-554-6759-8 (ISBN)
Public defence
2007-01-13, B42, BMC, Husargatan 3, Uppsala, 10:15
Opponent
Supervisors
Available from: 2006-12-22 Created: 2006-12-22Bibliographically approved

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Norgren, AnnaArvidsson, Per

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