Novel binding studies of human serum albumin with trans-feruloyl maslinic acid

Rajagopal Subramanyam, Mahesh Goud, Babu Sudhamalla, Eswarreddy Reddeem, Anilkishor Gollapudi, Sreedhar Nellaepalli, Venkateswarlu Yadavalli, Madhurarekha Chinnaboina, Damu G. Amooru

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Human serum albumin (HSA) is a predominant protein in the blood. Most drugs can bind to HSA and be transported to target locations of the body. For this study, we have extracted 3-trans-feruloyl maslinic acid (FMA) from the medicinal plant Tetracera asiatica, its a non-fluorescent derivative have potent anti-cancer, anti-HIV, anti-diabetic, and anti-inflammatory activities. The binding constant of the compound with HSA, calculated from fluorescence data, was found as KFMA = 1.42 ± 0.01 × 108 M-1, which corresponds to 10.9 kcal M-1 of free energy. Furthermore, microTOF-Q mass spectrometry data showed binding of FMA at nanomolar concentrations of FMA to free HSA. The study detected a mass increase from 66,560 Da (free HSA) to 67,919 Da (HSA + drug). This indicated a strong binding of FMA to HSA, resulting in an increase of the protein's absorbance and fluorescence. The secondary structure of HSA + FMA (0.1 mM) complexes showed the protein secondary structure became partially unfolded upon interaction of FMA with HSA, as well as indicating that HSA-FMA complexes were formed. Docking experiments uncovered the binding mode of FMA in HSA molecule. It was found that FMA binds strongly in different places with hydrogen bonding at IB domain of Arg 114, Leu 115 and Asp 173.

Original languageEnglish
Pages (from-to)81-88
Number of pages8
JournalJournal of Photochemistry and Photobiology B: Biology
Volume95
Issue number2
DOIs
Publication statusPublished - May 4 2009
Externally publishedYes

Fingerprint

albumins
Serum Albumin
serums
acids
proteins
drugs
maslinic acid
Fluorescence
Secondary Protein Structure
fluorescence
human immunodeficiency virus
Hydrogen Bonding
Medicinal Plants
Pharmaceutical Preparations
blood
Blood Proteins
Mass Spectrometry
Anti-Inflammatory Agents
mass spectroscopy
cancer

Keywords

  • Binding constant
  • Feruloyl maslinic acid
  • Fluorescence emission
  • Human serum albumin
  • Ligand binding
  • MicroTOF-Q mass spectrometry

ASJC Scopus subject areas

  • Radiation
  • Radiological and Ultrasound Technology
  • Biophysics
  • Radiology Nuclear Medicine and imaging

Cite this

Novel binding studies of human serum albumin with trans-feruloyl maslinic acid. / Subramanyam, Rajagopal; Goud, Mahesh; Sudhamalla, Babu; Reddeem, Eswarreddy; Gollapudi, Anilkishor; Nellaepalli, Sreedhar; Yadavalli, Venkateswarlu; Chinnaboina, Madhurarekha; Amooru, Damu G.

In: Journal of Photochemistry and Photobiology B: Biology, Vol. 95, No. 2, 04.05.2009, p. 81-88.

Research output: Contribution to journalArticle

Subramanyam, R, Goud, M, Sudhamalla, B, Reddeem, E, Gollapudi, A, Nellaepalli, S, Yadavalli, V, Chinnaboina, M & Amooru, DG 2009, 'Novel binding studies of human serum albumin with trans-feruloyl maslinic acid', Journal of Photochemistry and Photobiology B: Biology, vol. 95, no. 2, pp. 81-88. https://doi.org/10.1016/j.jphotobiol.2009.01.002
Subramanyam, Rajagopal ; Goud, Mahesh ; Sudhamalla, Babu ; Reddeem, Eswarreddy ; Gollapudi, Anilkishor ; Nellaepalli, Sreedhar ; Yadavalli, Venkateswarlu ; Chinnaboina, Madhurarekha ; Amooru, Damu G. / Novel binding studies of human serum albumin with trans-feruloyl maslinic acid. In: Journal of Photochemistry and Photobiology B: Biology. 2009 ; Vol. 95, No. 2. pp. 81-88.
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