NDLI: Effects of nanoparticle surface ligands on protein adsorption and subsequent cytotoxicity

Please wait, while we are loading the content...

Ibuprofen-loaded electrospun fibrous scaffold doped with sodium bicarbonate for responsively inhibiting inflammation and promoting muscle wound healing in vivo

Covalent attachment of multilayers (CAM): a platform for pH switchable antimicrobial and anticoagulant polymeric surfaces

Design and use of silica-containing redox nanoparticles, siRNPs, for high-performance peritoneal dialysis

Biodegradable nanoparticles composed of enantiomeric poly(γ-glutamic acid)-graft-poly(lactide) copolymers as vaccine carriers for dominant induction of cellular immunity

Toward a highly hemocompatible membrane for blood purification via a physical blend of miscible comb-like amphiphilic copolymers

Maintenance of ischemic β cell viability through delivery of lipids and ATP by targeted liposomes

Genetically encoded self-assembly of large amyloid fibers

A nanopatterned cell-seeded cardiac patch prevents electro-uncoupling and improves the therapeutic efficacy of cardiac repair

Long-term biostability and bioactivity of “fibrin linked” VEGF₁₂₁in vitro and in vivo

Back cover

Biomaterials Science Vol - 2 Issue - 3

Biomaterials Science Vol - 2 Issue - 2

Biomaterials Science Vol -1

Effects of nanoparticle surface ligands on protein adsorption and subsequent cytotoxicity

Content Provider	Royal Society of Chemistry (RSC)
Author	Bai, Jing Wang, Yichen Wang, Tiantian Jiang, Xiue
Copyright Year	2014
Abstract	With the widespread use of nanoparticles (NPs) such as quantum dots (QDs) in biomedical applications, and the growing concerns about nanotoxicity of these engineered nanoparticles, the importance of nanoparticle–protein interaction has not been well emphasized. In order to better understand the physical basis of the biological activity of nanoparticles in nanomedicine applications or under conditions of environmental exposure, the interaction of CdSe/ZnS QDs having different surface ligands as a model with human serum albumin (HSA) has been investigated in detail by various spectroscopic techniques including UV-vis absorption, fluorescence, circular dichroism, and Fourier transform infrared (FTIR) spectroscopies. We find that QDs coated with zwitterionic D-penicillamine (DPA-QDs) or anionic mercaptosuccinic acid (MSA-QDs) bind to the same site of serum albumin, domain II A, site I, and the differences of the Stern–Volmer quenching constant KSV and the binding constant K are about sixfold and sevenfold after 4 h of mixing, respectively. We also find tentative evidence that the model proteins undergo conformational changes upon association with the QDs that have different surface ligands. Additional cellular cytotoxicity assays, with HeLa cells, reveal that the stronger adsorption capacity of HSA on the surface of MSA-QDs results in more reduced cytotoxicity for the protein-coated QDs, while the weaker binding capacity of HSA on DPA-QDs has less effect on the interaction of QDs with cells. These findings have shed light on the design and application of QDs nanomaterials to nanomedicine by a comprehensive preconsideration of their interaction with human serum proteins.
Starting Page	493
Ending Page	501
Page Count	9
File Format	HTM / HTML PDF
ISSN	20474830
Volume Number	2
Issue Number	4
Journal	Biomaterials Science
DOI	10.1039/c3bm60224a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Human serum albumin Infrared spectroscopy Binding constant Volmer Fluorescence Fourier transform Cytotoxicity Nanomaterials Serum albumin Penicillamine KSV Circular dichroism HeLa Quantum Fourier Adsorption Carboxylic acid HSA Nanomedicine
Content Type	Text
Resource Type	Article
Subject	Materials Science Biomedical Engineering

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Deciphering the binding patterns and conformation changes upon the bovine serum albumin–rosmarinic acid complex

Binding of heme to human serum albumin: Steady-state fluorescence, circular dichroism and optical difference spectroscopic studies

Cell cytotoxicity and serum albumin binding capacity of the morin–Cu(ii) complex and its effect on deoxyribonucleic acid

Binding of a potential anti-hepatoma drug cis,cis,trans-[Pt(NH₃)₂Cl₂(O₂CCH₂CH₂COOH)-(OCONHC₁₆H₃₃)] with serum albumin – thermodynamic and conformational investigations

Biocompatible CdSe/ZnS quantum dot micelles for long-term cell imaging without alteration to the native structure of the blood plasma protein human serum albumin

Cellular response to chirality and amplified chirality

Spectroscopy characterization of the interaction between brevifolin carboxylic acid and bovine serum albumin.

Investigations into the bovine serum albumin binding and fluorescence properties of Tb (III) complex of a novel 8-hydroxyquinoline ligand.

Interactions of cucurbit[6,7]urils with human serum albumin and their effects on zaltoprofen transportation

Effects of nanoparticle surface ligands on protein adsorption and subsequent cytotoxicity

Similar Documents

Deciphering the binding patterns and conformation changes upon the bovine serum albumin–rosmarinic acid complex

Binding of heme to human serum albumin: Steady-state fluorescence, circular dichroism and optical difference spectroscopic studies

Cell cytotoxicity and serum albumin binding capacity of the morin–Cu(ii) complex and its effect on deoxyribonucleic acid

Binding of a potential anti-hepatoma drug cis,cis,trans-[Pt(NH3)2Cl2(O2CCH2CH2COOH)-(OCONHC16H33)] with serum albumin – thermodynamic and conformational investigations

Biocompatible CdSe/ZnS quantum dot micelles for long-term cell imaging without alteration to the native structure of the blood plasma protein human serum albumin

Cellular response to chirality and amplified chirality

Spectroscopy characterization of the interaction between brevifolin carboxylic acid and bovine serum albumin.

Investigations into the bovine serum albumin binding and fluorescence properties of Tb (III) complex of a novel 8-hydroxyquinoline ligand.

Interactions of cucurbit[6,7]urils with human serum albumin and their effects on zaltoprofen transportation

Effects of nanoparticle surface ligands on protein adsorption and subsequent cytotoxicity

Binding of a potential anti-hepatoma drug cis,cis,trans-[Pt(NH₃)₂Cl₂(O₂CCH₂CH₂COOH)-(OCONHC₁₆H₃₃)] with serum albumin – thermodynamic and conformational investigations