Structural Stability of Light-harvesting Protein LH2 Adsorbed on Mesoporous Silica Supports

Shibuya, Yotsugi; Itoh, Tetsuji; Matsuura, Shun-ichi; Yamaguchi, A.

doi:10.2116/analsci.31.1069

Cited by 9 publications

(17 citation statements)

References 24 publications

(35 reference statements)

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“…SBA-type mesoporous silica powders were synthesized using Pluronic ® P123 or Brij ® S10 as a template surfactant. 13,14 A hexagonal arrangement of one-dimensional pores was confirmed by small-angle X-ray (SAXS) profiles. The SAXS profiles were measured on a Rigaku SmartLab X-ray diffractometer.…”

Section: Materials and Chemicalsmentioning

confidence: 92%

Characterization of Myoglobin Adsorption into Mesoporous Silica Pores by Differential Scanning Calorimetry

et al. 2018

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Adsorption of protein molecules into the pores of a porous material is an important process for chromatographic separation of proteins and synthesis of nanoscale biocatalyst systems; however, there are barriers to developing a method for analyzing the process quantitatively. The purpose of this study is to examine the applicability of differential scanning calorimetry (DSC) for quantitative analysis of protein adsorption into silica mesopores. For this purpose myoglobin, a globular protein (diameter: 35.2 Å) was selected, and its adsorption onto mesoporous silica powders with uniform pore diameters (pore diameters: 39 and 64 Å) was measured by adsorption assay and DSC experiments. Our results confirmed that the adsorption of myoglobin into the silica mesopores induced significant changes in the positions and areas of freezing/melting peaks of the pore water. The decrease in heat of fusion of the pore water after myoglobin adsorption could be utilized to quantify the amount of myoglobin inside the silica mesopores. The advantages of DSC include its applicability to small wet mesoporous silica samples.

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Section: Materials and Chemicalsmentioning

confidence: 92%

Characterization of Myoglobin Adsorption into Mesoporous Silica Pores by Differential Scanning Calorimetry

et al. 2018

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“…On the other hand, no significant changes in the protein thermal stability upon adsorption were reported for watersoluble HSA 88 and OPH, 110 as well as membrane protein LH2. 114 Recently, it was reported that the thermal stability of myoglobin became lower upon adsorption at mesoporous silicas. 102 Enhanced thermal stabilities of proteins adsorbed at mesoporous silicas were likely explained by the configurational restriction and increased strength of the hydration of a protein molecule surrounded by a rigid pore wall, 113 hydrogen bonding between a protein molecule and the inner pore surface, 97 and heat transfer from matrices of a pore wall to a protein.…”

Section: Structural Stability Of Adsorbed Proteinmentioning

confidence: 99%

Structural Characterization of Proteins Adsorbed at Nanoporous Materials

et al. 2021

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A nanoporous material has been applied for the development of functional nanobiomaterials by utilizing its uniform pore structure and large adsorption capacity. The structure and stability of biomacromolecules, such as peptide, oligonucleotide, and protein, are primary factors to govern the performance of nanobiomaterials, so that their direct characterization methodologies are in progress. In this review, we focus on recent topics in the structural characterization of protein molecules adsorbed at a nanoporous material with uniform meso-sized pores. The thermal stabilities of the adsorbed proteins are also summarized to discuss whether the structure of the adsorbed protein molecules can be stabilized or not.

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“…In the absorption spectrum experiment, an integrating sphere was set just after the output window of the cryostat, and the transmitted light collected by the integrating sphere was detected. 28 …”

Section: Experimental Sectionmentioning

confidence: 99%

Differential Scanning Calorimetry Study on the Adsorption of Myoglobin at Mesoporous Silicas: Effects of Solution pH and Pore Size

et al. 2020

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In the present study, pore adsorption behavior of globular myoglobin (Mb) at mesoporous silicas was examined utilizing the low-temperature differential scanning calorimetry (DSC) method. The DSC method relies on a decrease in heat of fusion for the pore water upon adsorption of Mb. The amount and structure of Mb adsorbed into the mesoporous silica were examined by DSC and optical absorption spectroscopy. The results indicated that the pore adsorption behavior of Mb strongly depended on the solution pH and pore size of mesoporous silica. For the adsorption of Mb (diameter = 3.5 nm) into mesoporous silica with narrow pores (pore diameter = 3.3 nm) at a pH ranging from 7.0 to 3.7, the penetration of both folded and denatured Mb molecules was confirmed. The folded Mb could penetrate into large mesoporous silica pores (pore diameter = 5.3 and 7.9 nm), whereas the penetration of the denatured Mb molecules was completely inhibited. The distribution of folded Mb at mesoporous silica depended on the pore size; almost all folded Mb molecules located inside mesoporous silica pores of diameters 3.3 and 5.3 nm, whereas the Mb molecules distributed at bot internal and external pore surfaces of mesoporous silica with 7.9 nm in pore diameter. These pore adsorption behaviors suggest that aggregation or stacking of the Mb molecules at the pore entrance regions of the large pores affected the pore adsorption behavior.

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Structural Stability of Light-harvesting Protein LH2 Adsorbed on Mesoporous Silica Supports

Cited by 9 publications

References 24 publications

Characterization of Myoglobin Adsorption into Mesoporous Silica Pores by Differential Scanning Calorimetry

Characterization of Myoglobin Adsorption into Mesoporous Silica Pores by Differential Scanning Calorimetry

Structural Characterization of Proteins Adsorbed at Nanoporous Materials

Differential Scanning Calorimetry Study on the Adsorption of Myoglobin at Mesoporous Silicas: Effects of Solution pH and Pore Size

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