4.6 Article

Carbon Dots derived from Ocimum sanctum for dapsone-protein interactions: a quantitative approach

Journal

JOURNAL OF NANOSTRUCTURE IN CHEMISTRY
Volume -, Issue -, Pages -

Publisher

SPRINGER HEIDELBERG
DOI: 10.1007/s40097-022-00503-3

Keywords

Dapsone; Chromosomal aberration; E. coli; Allium sativum

Funding

  1. Najran University, Najran, Kingdom of Saudi Arabia [NU/RC/SERC/11/1]
  2. Council of Scientific and Industrial Research (CSIR), New Delhi [09/135(0894)/2019-EMR-I]
  3. DST [IFACH-17]
  4. Haryana State Council for Science and Technology [HSCSIT/RD/2020/476]
  5. DST Chandigarh
  6. DST
  7. UGC, India under the INDO-US 21st Century knowledge Initiative [194-2/2016 (IC)]

Ask authors/readers for more resources

This study investigates the use of carbon dots (CDs) as a drug carrier for the antileprosy drug dapsone (Dap). The study provides important information about the physicochemical interaction between the drug and serum albumins, as well as the release behavior of Dap from the Dap-CDs complex at different pH conditions.
The enthralling biocompatibility and low toxicity of carbon dots (CDs) has played progressive role in drug delivery. The present study aimed to use dapsone (Dap) as a model antileprosy drug and CDs as a drug carrier with a vision to enumerate a new and proficient means to study the physicochemical interaction of drug with serum albumins. The fluorescent CDs were fabricated by thermal calcination of a natural, nontoxic medicinal flower of Ocimum sanctum. The systematic surveillance of genotoxic studies on Allium sativum and gram-negative bacteria demonstrated the biocompatible nature of CDs in the used concentration ranges. The Dap molecules were anchored over the exterior surface of CDs via chemical interactions and then two different types of serum albumins were loaded on Dap-CDs complex by taking advantage of the electrostatic interactions. Furthermore, release behaviour of Dap from Dap-CDs complex at different pH conditions has been analysed. The apparent binding constant values between serum albumins with complex of Dap-CDs have further illustrated strong interaction between two components. Additionally, systematic information about the energetic of antileprosy drug-protein affinities over the surface of CDs as carried out in this work, is very important in providing detailed information for drug release behaviour. [GRAPHICS] .

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