Malaysian Journal of Analytical Sciences Vol 20 No 4 (2016): 735 - 740

DOI: http://dx.doi.org/10.17576/mjas-2016-2004-05

 

 

 

SPECTROSCOPIC CHARACTERIZATION OF COPPER(II)-BASED TETRAPEPTIDES

 

(Pencirian Spektroskopik Kuprum(II) Tetrapeptida)

 

Mohd. Basyaruddin Abdul Rahman1,2*, Sharifa Zaithun Begum1, Mohamed Ibrahim Mohamed Tahir2,

Haslina Ahmad1,2, Emilia Abdul Malek1,2

 

1Enzyme and Microbial Technology Research

2Department of Chemistry, Faculty of Science

Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia

 

*Corresponding author: basya@upm.edu.my

 

 

Received: 17 August 2015; Accepted: 7 May 2016

 

 

Abstract

Five different histidine and aspartic acid based tetrapeptides were designed using LOMETS and PyMol. They were chemically synthesized following the solid phase Fmoc-peptide synthesis protocols and were analysed using the reverse-phase High Performance Liquid Chromatography (HPLC) C18 analytical column for the purity. The peptides were further analysed by Liquid Chromatography Mass Spectrometry (LCMS) to see if the desired peptides were synthesized systematically. Copper(II) acetate monohydrate was bound to the peptides and the best molar ratio for the binding of these metal salts to peptides was 2:1. These observations were monitored through several spectroscopic techniques. The first physical observations for the successful synthesis of metallopeptides were the colour change, the melting/decomposition points and the solubility of these metallopeptides. Due to the visible colour change of the peptides to metallopeptides, UV-Visible spectroscopy and UV-Fluorescence spectroscopy were used as a qualitative analysis tests and the results were in agreement with other researchers’ data from similar researches.

 

Keywords: copper(II), histidine, aspartic acid, tetrapeptides, spectroscopic

 

Abstrak

Lima tetrapeptida berbeza yang mempunyai histidine dan asid aspartik direkabentuk oleh LOMETS dan PyMol. Tetrapeptida ini disintesis mengikut skim fasa pepejal peptida dan dianalisis menggunakan fasa sonsang Kromatografi Cecair Berprestasi Tinggi (HPLC) C18 turus analisis untuk mengetahui keaslian peptida. Kesemua peptida ini dianalisis mengunakan Kromatografi Cecair-Spektrometer Jisim (LC-MS) untuk mengkaji sintesis peptida secara sistematik. Kuprum(II) asetat monohidrat terikat kepada peptida dan nisbah mol yang terbaik untuk mengikat garam logam ini kepada peptida adalah 2:1. Cerapan ini telah dipantau melalui beberapa teknik spektroskopi. Pemerhatian fizikal pertama untuk logam peptida yang berjaya disintesis ialah perubahan warna, takat lebur/penguraian dan kebolehlarutan peptida logam ini. Oleh kerana perubahan warna yang nyata dalam dari peptida kepada logam peptida, spektroskopi Ultralembayung-tampak (UV-Vis) dan spektroskopi Ultralembayung-Pendafluor (UV-Fluorescence) digunakan sebagai ujian analisis kuantatif dan data yang diperolehi adalah setara dengan perolehan data bagi penyelidikan yang serupa.

 

 Kata kunci: Kuprum(II), histidin, asid aspartik, tetrapeptida, spektroskopi

 

References

1.       Ming, L. J. (2010). Metallopeptides from drug discovery to catalysis. Journal of Chinese Chemical Society, 57: 285 – 299.

2.       Ball, Z. T. and Zaykov, A. N. (2011). A general synthesis of dirhodium metallopeptides as MDM2 ligands. Chemical Communications, 47: 10927 – 10929.

3.       Tay, W. M (2010). Metallopeptides as model systems for the study of Cu(II)-dependent oxidation chemistry,  Thesis University of South Florida.

4.       Sambasivan, R. and Ball, Z. T. (2010). Metallopeptides for asymmetric dirhodium catalysis. Journal of the American Chemical Society. 132: 9289 – 9295.

5.       Karavelas, T., Mylonas, M., Malandrinos, G., Plakatouras, J. C., Hadjiliadis, N., Mlynarz, P. and Kozlowski, H. (2005). Coordination properties of Cu(II) and Ni(II) ions towards the C-terminal peptide fragment -ELAKHA- of histone H2B. Journal of Inorganic Biochemistry. 99(2): 606 – 615.

6.       Neupane, K. P, Aldous, A. R. and Kritzer, J. A. (2013). Macrocyclization of the ATCUN motif controls metal binding and catalysis. Inorganic Chemistry. 52(5): 2729 – 2735.

7.       Boka, B., Myari, A., Sovago, I. and Hadjiliadis, N. (2004). Copper(II) and zinc(II) complexes of the peptides Ac-HisValHis-NH2 and Ac-HisValGlyAsp-NH2 related to the active site of the enzyme CuZnSOD. Journal of Inorganic Biochemistry. 98(1): 113 – 122.

8.       Penner, M. H. (2010). Ultraviolet, visible and fluorescence spectroscopy. In Food Analysis, 4th Ed., Suzanne Nielsen, Ed. Springer.

9.       Goulding, A.M. (2010). Biochemical applications of DsRed-Monomer utilizing fluorescence and metal-binding affinity. Unpublished doctoral dissertation, Purdue University, Indianapolis, Indiana.

10.    Deo, S.K., Rahimi, Y., Goulding, A., Shrestha, S., Mirpuri, S. (2008). Mechanism of copper induced fluorescence quenching of red fluorescent protein, DsRed. Biochemical and Biophysicsal Research Communication. 370(1): 57 – 61.

 




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