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Aloe emodin, an anthroquinone from Aloe vera acts as an anti aggregatory agent to the thermally aggregated hemoglobin.
Furkan, Mohammad; Alam, Md Tauqir; Rizvi, Asim; Khan, Kashan; Ali, Abad; Naeem, Aabgeena.
Affiliation
  • Furkan M; Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, India.
  • Alam MT; Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, India.
  • Rizvi A; Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, India.
  • Khan K; Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, India.
  • Ali A; Department of Chemistry, Faculty of Science, Aligarh Muslim University, Aligarh 202002, India.
  • Shamsuzzaman; Department of Chemistry, Faculty of Science, Aligarh Muslim University, Aligarh 202002, India.
  • Naeem A; Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, India. Electronic address: aabgeenanaim@gmail.com.
Spectrochim Acta A Mol Biomol Spectrosc ; 179: 188-193, 2017 May 15.
Article in En | MEDLINE | ID: mdl-28242448
ABSTRACT
Aggregation of proteins is a physiological process which contributes to the pathophysiology of several maladies including diabetes mellitus, Huntington's and Alzheimer's disease. In this study we have reported that aloe emodin (AE), an anthroquinone, which is one of the active components of the Aloe vera plant, acts as an inhibitor of hemoglobin (Hb) aggregation. Hb was thermally aggregated at 60°C for four days as evident by increased thioflavin T and ANS fluorescence, shifted congo red absorbance, appearance of ß sheet structure, increase in turbidity and presence of oligomeric aggregates. Increasing concentration of AE partially reverses the aggregation of the model heme protein (hemoglobin). The maximum effect of AE was observed at 100µM followed by saturation at 125µM. The results were confirmed by UV-visible spectrometry, intrinsic fluorescence, ThT, ANS, congo red assay as well as transmission electron microscopy (TEM). These results were also supported by fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) which shows the disappearance of ß sheet structure and appearance of α helices. This study will serve as baseline for translatory research and the development of AE based therapeutics for diseases attributed to protein aggregation.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Temperature / Hemoglobins / Anthraquinones / Aloe / Protein Aggregates Limits: Animals Language: En Journal: Spectrochim Acta A Mol Biomol Spectrosc Journal subject: BIOLOGIA MOLECULAR Year: 2017 Document type: Article Affiliation country: India

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Temperature / Hemoglobins / Anthraquinones / Aloe / Protein Aggregates Limits: Animals Language: En Journal: Spectrochim Acta A Mol Biomol Spectrosc Journal subject: BIOLOGIA MOLECULAR Year: 2017 Document type: Article Affiliation country: India