In silico modeling and experimental evidence of coagulant protein interaction with precursors for nanoparticle functionalization
2013 (English)In: Journal of Biomolecular Structure and Dynamics, ISSN 0739-1102, Vol. 31, no 10, 1182-1190 p.Article in journal (Refereed) Published
The design of novel protein-nanoparticle hybrid systems has applications in many fields of science ranging from biomedicine, catalysis, water treatment, etc. The main barrier in devising such tool is lack of adequate information or poor understanding of protein-ligand chemistry. Here, we establish a new strategy based on computational modeling for protein and precursor linkers that can decorate the nanoparticles. Moringa oleifera (MO2.1) seed protein that has coagulation and antimicrobial properties was used. Superparamagnetic nanoparticles (SPION) with precursor ligands were used for the protein-ligand interaction studies. The molecular docking studies reveal that there are two binding sites, one is located at the core binding site; tetraethoxysilane (TEOS) or 3-aminopropyl trimethoxysilane (APTES) binds to this site while the other one is located at the side chain residues where trisodium citrate (TSC) or Si-60 binds to this site. The protein-ligand distance profile analysis explains the differences in functional activity of the decorated SPION. Experimentally, TSC-coated nanoparticles showed higher coagulation activity as compared to TEOS- and APTES-coated SPION. To our knowledge, this is the first report on in vitro experimental data, which endorses the computational modeling studies as a powerful tool to design novel precursors for functionalization of nanomaterials; and develop interface hybrid systems for various applications.
Place, publisher, year, edition, pages
2013. Vol. 31, no 10, 1182-1190 p.
molecular docking, magnetic nanoparticle, Moringa oleifera, surface coating, coagulation activity, binding free energy
IdentifiersURN: urn:nbn:se:kth:diva-94166DOI: 10.1080/07391102.2012.726534ISI: 000324002100014ScopusID: 2-s2.0-84884565897OAI: oai:DiVA.org:kth-94166DiVA: diva2:525683
QC 20131004. Updated from submitted to published.2012-05-092012-05-092013-10-18Bibliographically approved