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Glycosylated Foldamers: Synthesis of Carbohydrate-modified β3hSer and Incorporation into β-Peptides
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.
2007 (English)In: Journal of Peptide Science, ISSN 1075-2617, E-ISSN 1099-1387, Vol. 13, no 11, 717-727 p.Article in journal (Refereed) Published
Abstract [en]

Fmoc-protected β3hserine (β3hSer) was prepared and O-linked to suitably protected N-acetylgalactosamine (GalNAc) and N-acetylglucosamine (GlcNAc) derivatives. Glycosylation of β3hSer was made by two independent routes: either by direct glycosyl linkage to the β3hSer, or linkage to natural L-Ser and then utilizing the carbohydrate moiety as a protecting group in an Arndt–Eistert homologation. Both procedures gave the novel glycosylated β3-amino acids Fmoc-β3hSer(α-D-GalNAc(Ac)3)-OH (1a), its β-anomer (1b), and Fmoc-β3hSer(β-D-GlcNAc(Ac)3)-OH (2), which were utilized in the solid-phase peptide synthesis of four glycosylated dipeptides (3a–d) and two heptapeptides (4a–b). The preparation of β-amino acids bearing common post-translational modifiers represents an important step towards functionalized foldamers with broad applications in biomedical research.

Place, publisher, year, edition, pages
2007. Vol. 13, no 11, 717-727 p.
National Category
Natural Sciences
URN: urn:nbn:se:uu:diva-95278DOI: 10.1002/psc.832ISI: 000252622900004PubMedID: 17890640OAI: oai:DiVA.org:uu-95278DiVA: diva2:169437
Available from: 2006-12-22 Created: 2006-12-22 Last updated: 2015-08-19Bibliographically 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.
Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, ISSN 1651-6214 ; 253
Organic chemistry, Conformational investigations, β-peptides, glycosylation, biomolecular recognition, cyclic β³-peptides, cyclic mixed α/β²-peptides, β-peptoids, Organisk kemi
urn:nbn:se:uu:diva-7420 (URN)91-554-6759-8 (ISBN)
Public defence
2007-01-13, B42, BMC, Husargatan 3, Uppsala, 10:15
Available from: 2006-12-22 Created: 2006-12-22Bibliographically approved

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Arvidsson, Per I.
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