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Your search keyword '"Loai Al-Jamri"' showing total 2 results
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2 results on '"Loai Al-Jamri"'

1. Synthesis ofN?-Boc-N?-tetrabenzyl-DTPA-L-lysine andN?-Fmoc-N?-tetra-t-butyl-DTPA-L-lysine, building blocks for solid phase synthesis of DTPA-containing peptides

Author

Loai Al-Jamri and John S. Davies

Subjects
Pharmacology, chemistry.chemical_classification, biology, Stereochemistry, Chemistry, Ligand, organic chemicals, Metal ions in aqueous solution, Organic Chemistry, Lysine, Peptide, General Medicine, biology.organism_classification, Biochemistry, Medicinal chemistry, Acylation, Solid-phase synthesis, Structural Biology, Drug Discovery, Molecular Medicine, Tetra, Chelation, Molecular Biology
Abstract

Two building blocks, Boc-Lys(Bn4-DTPA)-OH and Fmoc-Lys(-DTPA)-OH have been synthesized via the acylation of the e-amino group of Nα-protected lysine, using suitably protected tetra-esters of diethylene triamine pentaacetic acid (DTPA), a ligand with wide application as a chelating agent for complexing metal ions to peptides. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.

Published
2002
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2. The synthesis and properties of Gla- and Phe-containing analogues of cyclic RGD pentapeptides

Author

Christian Naumer, Christine Enjalbal, John S. Davies, Corrine Nguyen, and Loai Al-Jamri

Subjects
Residue (chemistry), Integrin receptors, law, Stereochemistry, Chemistry, Recombinant DNA, Cyclic RGD, Cell adhesion, Combinatorial chemistry, law.invention
Abstract

Cyclopentapeptides containing the Arg-Gly-Asp motif have been synthesised using solid-phase assembly of side-chain-protected linear precursors, followed by solution-phase cyclisation. The replacement of the Asp residue by γ-carboxyglutamic acid (Gla) is a novel feature which gives rise to an analogue which inhibits cell adhesion, yet its congeners do not show activity in binding assays with recombinant integrin receptors. NMR techniques support a β/γ-turn conformation in most of the analogues.

Published
2000
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