Abstract
Solid-phase peptide synthesis of dipeptide (histidine-β-alanine) as a chelating agent examined by common N-9-fluorenylmethyloxycarbonyl-N-trityl-L-histidine and tert-butyloxycarbonyl-β-alanine-OH amino acid derivatives. Trityl chloride resin was used as a carrier resin. The molecular structure of the dipeptide was definite by using different methods such as ultraviolet visible (UV-Vis), Fourier transform infrared (FTIR), proton (1H) nuclear magnetic ressonance (NMR) and liquid chromatography-mass spectrometry (LC-MS) and the chelating property of synthesized dipeptide was investigated for removing of metal ions Al3+, Cu2+, Hg2+ and Pb2+in vitro. In addition, the pharmacological and biological activities of dipeptide were examined by prediction of activity spectra for substances (PASS) program.
Highlights
Peptides are one of the best candidates for drug development due to their high specificity and low toxicity
We report the synthesis of dipeptide histidine-β-alanine as a chelating agent with chemical method, solid-phase peptide synthesis
The results show that the maximum peaks were appeared at 214 and 264 nm, which can be assigned to π→π* and n→π*, respectively
Summary
Peptides are one of the best candidates for drug development due to their high specificity and low toxicity. Peptides are mostly obtained by biological technology or chemical synthesis. The chemical method, especially solidphase peptide synthesis (SPPS), is usually used for the large-scale production of peptides because of its simplified reaction procedure and easy purification/isolation steps for the target products.[1] SPPS can be defined as a process in which amino acid bound by its C-terminus to an insoluble polymer.[2] This method has made peptide synthesis simple, rapid, and subject to automation.[3] Protection of α- and β-amino functionality of amino acids is one of the most important issues in peptide chemistry and is efficient to prevent polymerization of the amino acid once it is activated. Both in solution and on solid-phase, are carried out in the C to N direction, α- and β-amino protecting groups are removed several
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