Effect of Salt on the Formation of Alcohol-Dehydrogenease Monolayer: A Study by the Langmuir−Blodgett Technique

Kamilya, Tapanendu; Pal, Prabir; Mahato, Mrityunjoy; Talapatra, G. B.

doi:10.1021/jp9001059

Cited by 30 publications

(41 citation statements)

References 55 publications

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“…The salt ions would have a stronger attraction with the highly polar water molecules than the less polar protein molecules [52]. Also, ion-protein dispersion potentials originating from the polarizabilities of ions and hIAPP could be involved in the salting-out effect [50].…”

Section: Langmuir Monolayer Preparationmentioning

confidence: 99%

Human islet amyloid polypeptide at the air–aqueous interface: a Langmuir monolayer approach

Mićić

Orbulescu

et al. 2012

J. R. Soc. Interface.

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Human islet amyloid polypeptide (hIAPP) is the source of the major component of the amyloid deposits found in the islets of Langerhans of around 95 per cent type 2 diabetic patients. The formation of aggregates and mature fibrils is thought to be responsible for the dysfunction and death of the insulin-producing pancreatic b-cells. Investigation on the conformation, orientation and self-assembly of the hIAPP at time zero could be beneficial for our understanding of its stability and aggregation process. To obtain these insights, the hIAPP at time zero was studied at the air-aqueous interface using the Langmuir monolayer technique. The properties of the hIAPP Langmuir monolayer at the air -aqueous interface on a NaCl subphase with pH 2.0, 5.6 and 9.0 were examined by surface pressure-and potential-area isotherms, UV-Vis absorption, fluorescence spectroscopy and Brewster angle microscopy. The conformational and orientational changes of the hIAPP Langmuir monolayer under different surface pressures were characterized by p-polarized infrared-reflection absorption spectroscopy, and the results did not show any prominent changes of conformation or orientation. The predominant secondary structure of the hIAPP at the air -aqueous interface was a-helix conformation, with a parallel orientation to the interface during compression. These results showed that the hIAPP Langmuir monolayer at the air -aqueous interface was stable, and no aggregate or domain of the hIAPP at the air -aqueous interface was observed during the time of experiments.

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Section: Langmuir Monolayer Preparationmentioning

confidence: 99%

Human islet amyloid polypeptide at the air–aqueous interface: a Langmuir monolayer approach

Mićić

Orbulescu

et al. 2012

J. R. Soc. Interface.

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“…This is generally, done by Gaussian fitting to describe the components [40]. A multiple peak fitting technique with Gaussian profile was employed to fit normalized amide-I band that allows one to identify and determine the peak frequencies of different components [41]. In addition, the percentage area of the corresponding deconvoluted peaks gives the relative amount of conformers.…”

Section: Ftir Studymentioning

confidence: 99%

Adsorption of pepsin in octadecylamine matrix at air–water interface

Kamilya

Pal

Talapatra

2010

Biophysical Chemistry

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“…FTIR analysis of the amide I band of protein was carried out to determine the secondary structure of Hb . ZnO NP binding‐associated unfolding of Hb was analyzed by fitting the amide I band (1600–1700 cm −1 ) using the FTIR spectrum.…”

Section: Resultsmentioning

confidence: 99%

Microscopic and spectroscopic study of the corona formation and unfolding of human haemoglobin in presence of ZnO nanoparticles

Bhunia

Saha

Kamilya³

2019

Luminescence

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The interaction of zinc oxide nanoparticles (ZnO NPs) with human haemoglobin (Hb) is studied for the biologically safe application of ZnO NPs in the human body. The Hb corona is formed around the ZnO nanoparticles, directly observed from highresolution transmission electron microscopy (HRTEM) images. Hb formed 'hard corona' on the surface of ZnO NPs from an exponential association mechanism over a very short duration, as well as unfolding of Hb that occurred over a long lifetime.Dynamic light scattering measurements demonstrated that the ZnO NPs were completely covered by Hb with shell thickness of c. 6 nm that formed a 'hard corona'.Zeta potential measurements represented that the ZnO NPs were fully covered by Hb molecules using an exponential association mechanism. Tryptophans (TRY), as well as heme-porphyrin moieties of Hb, are the major binding sites for ZnO NPs.The nature of the interaction between ZnO NPs and Hb was analysed from the fluorescence quenching of TRYs. Electrostatic interaction, along with the hydrophobic interaction between ZnO NPs and Hb, is responsible for the conformational change in Hb due to increase in the percentage of β-sheets together with a decrease in αhelices.

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Effect of Salt on the Formation of Alcohol-Dehydrogenease Monolayer: A Study by the Langmuir−Blodgett Technique

Cited by 30 publications

References 55 publications

Human islet amyloid polypeptide at the air–aqueous interface: a Langmuir monolayer approach

Human islet amyloid polypeptide at the air–aqueous interface: a Langmuir monolayer approach

Adsorption of pepsin in octadecylamine matrix at air–water interface

Microscopic and spectroscopic study of the corona formation and unfolding of human haemoglobin in presence of ZnO nanoparticles

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