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Design, synthesis, tandem mass spectrometric sequencing and biological activity of NGF mimetics
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Organic Pharmaceutical Chemistry.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Organic Pharmaceutical Chemistry.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Organic Pharmaceutical Chemistry.
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1996 (English)In: International journal of peptide & protein research, ISSN 0367-8377, Vol. 48, no 4, 337-346 p.Article in journal (Refereed) Published
Abstract [en]

Nine low molecular weight nerve growth factor (NGF)-like peptides have been designed to mimic the putative receptor-binding epitope of NGF defined by two beta-hairpin loops. Eight different spacers were used as variable links between the beta-loop amino acid residues, which from mutagenesis experiments were found to play an important role in the biological activity of NGF. These spacers were amino acids, natural or non-natural, differing in length (5-13 A) and polarity. The peptides were synthesized via the Fmoc solid-phase peptide synthesis and purified by reversed-phase HPLC. Their primary sequences were analyzed by a combination of automated Edman degradation and mass spectrometry. The peptides were tested using two different biological assays, the fibre outgrowth from chick embryonic sympathetic ganglia and the PC12 cell differentiation assay. Weak antagonistic effects could be observed for some peptides.

Place, publisher, year, edition, pages
1996. Vol. 48, no 4, 337-346 p.
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Medical and Health Sciences
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URN: urn:nbn:se:uu:diva-51180PubMedID: 8919054OAI: oai:DiVA.org:uu-51180DiVA: diva2:79089
Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2012-02-28Bibliographically approved

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