FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2912856690> ?p ?o ?g. }

• W2912856690 endingPage "165" @default.
• W2912856690 startingPage "156" @default.
• W2912856690 abstract "Heavy metal free and non-toxic semiconductor nanocrystals are the most interested segment of the current bio-nanotechnology. In the present paper, structural changes of human serum albumin (HSA) upon its interaction with InP/ZnS QDs coated with amphilic poly ethylene glycol was probed by employing multi-spectroscopic tools. Steady state and time resolved fluorescence studies implied formation of non-fluorescent complex between HSA and QDs resulting out of static quenching. Interestingly, temperature dependent fluorescence quantitative studies show that at higher temperatures these bioconjugates are unstable and static quenching mechanism turns towards dynamic quenching as QDs diffuses through excited state of HSA. Binding and synchronous fluorescence spectroscopic analysis show that QDs binds predominantly to Trp-214 residue in the HSA subdomain IIA with hydrophobic forces. Hence, observed blue shift of about 5 nm in PL spectra of HSA is the clear sign of conformational deformation as the Trp-214 residue gradually enters into hydrophobic microenvironment during its conjugation with QDs. Energy transfer efficiency (ET), transfer rate (KT) and critical transfer distance (R0) were all calculated for HSA and PEG-InP/ZnS QDs system from Förster resonance energy transfer (FRET) studies. Gibb's free energy, enthalpy and entropy obtained from temperature dependent fluorescence studies implied, HSA-InP/ZnS QDs bioconjugation is spontaneous, endothermic, entropy driven and is in accordance with the second law of thermodynamics. Hill coefficient (n ≅ 1) and binding affinities (kb) confirmed strong binding of HSA to QDs surface through ‘non-cooperative interactions’. Also, experimental result of FTIR spectra confirmed the adsorption of HSA onto the surfaces of PEG-InP/ZnS QDs. In addition these results proves that greener, heavy metal free and non-toxic semiconductor nanoparticle (PEG-InP/ZnS QDs) can potentially replace heavy metal and toxic QDs in biophysical fields like conformational studies of proteins." @default.
• W2912856690 created "2019-02-21" @default.
• W2912856690 creator A5019585519 @default.
• W2912856690 creator A5055050668 @default.
• W2912856690 creator A5073460991 @default.
• W2912856690 date "2019-05-01" @default.
• W2912856690 modified "2023-09-26" @default.
• W2912856690 title "Interaction between human serum albumin and toxic free InP/ZnS QDs using multi-spectroscopic study: An excellent alternate to heavy metal based QDs" @default.
• W2912856690 cites W1504792186 @default.
• W2912856690 cites W1581858536 @default.
• W2912856690 cites W1820760012 @default.
• W2912856690 cites W1963491340 @default.
• W2912856690 cites W1963745089 @default.
• W2912856690 cites W1967321494 @default.
• W2912856690 cites W1975421678 @default.
• W2912856690 cites W1976480102 @default.
• W2912856690 cites W1980599353 @default.
• W2912856690 cites W1983588291 @default.
• W2912856690 cites W1990379353 @default.
• W2912856690 cites W1997526812 @default.
• W2912856690 cites W2005967929 @default.
• W2912856690 cites W2008390690 @default.
• W2912856690 cites W2009805582 @default.
• W2912856690 cites W2013557720 @default.
• W2912856690 cites W2017654147 @default.
• W2912856690 cites W2019556240 @default.
• W2912856690 cites W2021485828 @default.
• W2912856690 cites W2026732393 @default.
• W2912856690 cites W2027175712 @default.
• W2912856690 cites W2031715022 @default.
• W2912856690 cites W2032217327 @default.
• W2912856690 cites W2032860659 @default.
• W2912856690 cites W2034053896 @default.
• W2912856690 cites W2034703350 @default.
• W2912856690 cites W2038980827 @default.
• W2912856690 cites W2040265643 @default.
• W2912856690 cites W2041775518 @default.
• W2912856690 cites W2042191284 @default.
• W2912856690 cites W2042391719 @default.
• W2912856690 cites W2052230935 @default.
• W2912856690 cites W2053302198 @default.
• W2912856690 cites W2062485439 @default.
• W2912856690 cites W2063575064 @default.
• W2912856690 cites W2067231961 @default.
• W2912856690 cites W2067557497 @default.
• W2912856690 cites W2079094085 @default.
• W2912856690 cites W2079208082 @default.
• W2912856690 cites W2082454728 @default.
• W2912856690 cites W2088900329 @default.
• W2912856690 cites W2090966581 @default.
• W2912856690 cites W2091310878 @default.
• W2912856690 cites W2104571730 @default.
• W2912856690 cites W2104659028 @default.
• W2912856690 cites W2107208446 @default.
• W2912856690 cites W2127068865 @default.
• W2912856690 cites W2129378094 @default.
• W2912856690 cites W2133611926 @default.
• W2912856690 cites W2137491407 @default.
• W2912856690 cites W2147418373 @default.
• W2912856690 cites W2148250405 @default.
• W2912856690 cites W2148357165 @default.
• W2912856690 cites W2154321074 @default.
• W2912856690 cites W2155916246 @default.
• W2912856690 cites W2164551466 @default.
• W2912856690 cites W2188225019 @default.
• W2912856690 cites W2219643139 @default.
• W2912856690 cites W2284220832 @default.
• W2912856690 cites W2324523442 @default.
• W2912856690 cites W2329957751 @default.
• W2912856690 cites W2418604120 @default.
• W2912856690 cites W2765862805 @default.
• W2912856690 cites W2952253429 @default.
• W2912856690 doi "https://doi.org/10.1016/j.molliq.2019.02.041" @default.
• W2912856690 hasPublicationYear "2019" @default.
• W2912856690 type Work @default.
• W2912856690 sameAs 2912856690 @default.
• W2912856690 citedByCount "13" @default.
• W2912856690 countsByYear W29128566902021 @default.
• W2912856690 countsByYear W29128566902022 @default.
• W2912856690 countsByYear W29128566902023 @default.
• W2912856690 crossrefType "journal-article" @default.
• W2912856690 hasAuthorship W2912856690A5019585519 @default.
• W2912856690 hasAuthorship W2912856690A5055050668 @default.
• W2912856690 hasAuthorship W2912856690A5073460991 @default.
• W2912856690 hasConcept C113196181 @default.
• W2912856690 hasConcept C121332964 @default.
• W2912856690 hasConcept C121745418 @default.
• W2912856690 hasConcept C14631669 @default.
• W2912856690 hasConcept C155672457 @default.
• W2912856690 hasConcept C171250308 @default.
• W2912856690 hasConcept C178790620 @default.
• W2912856690 hasConcept C185592680 @default.
• W2912856690 hasConcept C192562407 @default.
• W2912856690 hasConcept C2778597219 @default.
• W2912856690 hasConcept C43617362 @default.
• W2912856690 hasConcept C62520636 @default.
• W2912856690 hasConcept C75473681 @default.
• W2912856690 hasConcept C91881484 @default.

• next