Comprehensive spectroscopic studies of synergism between Gadong starch based carbon dots and bovine serum albumin

Regina Sisika A. Sonthanasamy, Nik Muslihuddin Nik Sulaiman, Ling Ling Tan @ Chong, Mohamad Azwani Shah Mat Lazim

Research output: Contribution to journalArticle

Abstract

Carbon dots (C-dots) were used to study the binding mechanisms with serum protein, bovine serum albumin (BSA) by using two notable binding systems known as non-covalent and covalent interaction. Interaction between C-dots and BSA were estimated by Stern-Volmer equation and Double Log Regression Model (DLRM). According to the fluorescent intensity, quenching of model carrier protein by C-dots was due to dynamic quenching for non-covalent and static quenching for covalent binding. The binding site constant, K A and number of binding site, for covalent interaction is 1754.7 L/mol and n ≈ 1 (0.6922) were determined by DLRM on fluorescence quenching results. The blue shift of the fluorescence spectrum, from 450 nm to 421 nm (non-covalent) and 430 nm (covalent) and suggested that both the microenvironment of C-dots and protein changed in relation to the protein concentration. The fluorescence intensity results show that protein structure has a significant role in Protein-C-dots interactions and type of binding influence physicochemical properties of C-dots differently. Understanding to this bio interface is important to utilize both quantum dots and biomolecules for biomedical field. It can be a useful guideline to design further applications in biomedical and bioimaging.

Original languageEnglish
Pages (from-to)85-96
Number of pages12
JournalSpectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
Volume218
DOIs
Publication statusPublished - 5 Jul 2019

Fingerprint

starches
Bovine Serum Albumin
Starch
albumins
serums
Carbon
proteins
carbon
Quenching
Proteins
quenching
Fluorescence
Binding sites
fluorescence
regression analysis
Binding Sites
interactions
Biomolecules
blue shift
Semiconductor quantum dots

Keywords

  • Binding interaction
  • Bovine serum albumin
  • C-dots
  • Fluorescence quenching
  • Quantum dots

ASJC Scopus subject areas

  • Analytical Chemistry
  • Atomic and Molecular Physics, and Optics
  • Instrumentation
  • Spectroscopy

Cite this

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abstract = "Carbon dots (C-dots) were used to study the binding mechanisms with serum protein, bovine serum albumin (BSA) by using two notable binding systems known as non-covalent and covalent interaction. Interaction between C-dots and BSA were estimated by Stern-Volmer equation and Double Log Regression Model (DLRM). According to the fluorescent intensity, quenching of model carrier protein by C-dots was due to dynamic quenching for non-covalent and static quenching for covalent binding. The binding site constant, K A and number of binding site, for covalent interaction is 1754.7 L/mol and n ≈ 1 (0.6922) were determined by DLRM on fluorescence quenching results. The blue shift of the fluorescence spectrum, from 450 nm to 421 nm (non-covalent) and 430 nm (covalent) and suggested that both the microenvironment of C-dots and protein changed in relation to the protein concentration. The fluorescence intensity results show that protein structure has a significant role in Protein-C-dots interactions and type of binding influence physicochemical properties of C-dots differently. Understanding to this bio interface is important to utilize both quantum dots and biomolecules for biomedical field. It can be a useful guideline to design further applications in biomedical and bioimaging.",
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author = "Sonthanasamy, {Regina Sisika A.} and Sulaiman, {Nik Muslihuddin Nik} and {Tan @ Chong}, {Ling Ling} and {Mat Lazim}, {Mohamad Azwani Shah}",
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AU - Mat Lazim, Mohamad Azwani Shah

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AB - Carbon dots (C-dots) were used to study the binding mechanisms with serum protein, bovine serum albumin (BSA) by using two notable binding systems known as non-covalent and covalent interaction. Interaction between C-dots and BSA were estimated by Stern-Volmer equation and Double Log Regression Model (DLRM). According to the fluorescent intensity, quenching of model carrier protein by C-dots was due to dynamic quenching for non-covalent and static quenching for covalent binding. The binding site constant, K A and number of binding site, for covalent interaction is 1754.7 L/mol and n ≈ 1 (0.6922) were determined by DLRM on fluorescence quenching results. The blue shift of the fluorescence spectrum, from 450 nm to 421 nm (non-covalent) and 430 nm (covalent) and suggested that both the microenvironment of C-dots and protein changed in relation to the protein concentration. The fluorescence intensity results show that protein structure has a significant role in Protein-C-dots interactions and type of binding influence physicochemical properties of C-dots differently. Understanding to this bio interface is important to utilize both quantum dots and biomolecules for biomedical field. It can be a useful guideline to design further applications in biomedical and bioimaging.

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