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Article ; Online: Correlation between Hydration States and Self-assembly Structures of Phospholipid and Surfactant Studied by Terahertz Spectroscopy.

Hishida, Mafumi

2024 Volume 73, Issue 4, Page(s) 419–427

Abstract: Phospholipids and surfactants form membranes and other self-assembled structures in water. However, it is not fully understood how the surrounding water (hydration water) is involved in their structure formation. In this paper, I summarize the results of ...

Abstract	Phospholipids and surfactants form membranes and other self-assembled structures in water. However, it is not fully understood how the surrounding water (hydration water) is involved in their structure formation. In this paper, I summarize the results of our investigation of the long-range hydration state of phospholipids and surfactants at their surfaces by means of terahertz spectroscopy. By observing the collective rotational dynamics of water in the picosecond time scale, this technique allows us to observe not only the water directly bound to the solute, but also the weakly affected water outside of it. For example, PC phospholipids inhibit water dynamics over long distances, whereas PE phospholipids make water more mobile than bulk water. The causes of this difference in hydration and how it is involved in the structural formation of the membrane are reviewed.
MeSH term(s)	Lipoproteins ; Phospholipids/chemistry ; Pulmonary Surfactants ; Surface-Active Agents ; Terahertz Spectroscopy/methods ; Water/chemistry
Chemical Substances	Lipoproteins ; Phospholipids ; Pulmonary Surfactants ; Surface-Active Agents ; Water (059QF0KO0R)
Language	English
Publishing date	2024-03-27
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	2218264-0
ISSN	1347-3352 ; 1345-8957
ISSN (online)	1347-3352
ISSN	1345-8957
DOI	10.5650/jos.ess23188
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Contrasting Changes in Strongly and Weakly Bound Hydration Water of a Protein upon Denaturation.

Hishida, Mafumi / Kaneko, Ayumi / Yamamura, Yasuhisa / Saito, Kazuya

The journal of physical chemistry. B

2023 Volume 127, Issue 28, Page(s) 6296–6305

Abstract: Water is considered integral for the stabilization and function of proteins, which has recently attracted significant attention. However, the microscopic aspects of water ranging up to the second hydration shell, including strongly and weakly bound water ...

Abstract	Water is considered integral for the stabilization and function of proteins, which has recently attracted significant attention. However, the microscopic aspects of water ranging up to the second hydration shell, including strongly and weakly bound water at the sub-nanometer scale, are not yet well understood. Here, we combined terahertz spectroscopy, thermal measurements, and infrared spectroscopy to clarify how the strongly and weakly bound hydration water changes upon protein denaturation. With denaturation, that is, the exposure of hydrophobic groups in water and entanglement of hydrophilic groups, the number of strongly bound hydration water decreased, while the number of weakly bound hydration water increased. Even though the constraint of water due to hydrophobic hydration is weak, it extends to the second hydration shell as it is caused by the strengthening of hydrogen bonds between water molecules, which is likely the key microscopic mechanism for the destabilization of the native state due to hydration.
MeSH term(s)	Water/chemistry ; Proteins/chemistry ; Hydrophobic and Hydrophilic Interactions ; Hydrogen Bonding ; Protein Denaturation
Chemical Substances	Water (059QF0KO0R) ; Proteins
Language	English
Publishing date	2023-07-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1520-5207
ISSN (online)	1520-5207
DOI	10.1021/acs.jpcb.3c02970
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Article ; Online: Effect of Osmolytes on Water Mobility Correlates with Their Stabilizing Effect on Proteins.

Hishida, Mafumi / Anjum, Rubaiya / Anada, Takahisa / Murakami, Daiki / Tanaka, Masaru

The journal of physical chemistry. B

2022 Volume 126, Issue 13, Page(s) 2466–2475

Abstract: There is a long, ongoing debate on how small molecules (osmolytes) affect the stability of proteins. The present study found that change in collective rotational dynamics of water in osmolyte solutions likely has a dominant effect on protein denaturation. ...

Abstract	There is a long, ongoing debate on how small molecules (osmolytes) affect the stability of proteins. The present study found that change in collective rotational dynamics of water in osmolyte solutions likely has a dominant effect on protein denaturation. According to THz spectroscopy analysis, osmolytes that stabilize proteins are accompanied by bound hydration water with slow dynamics, while the collective rotational dynamics of water is accelerated in the case of denaturant osmolytes. Among 15 osmolytes studied here, there is a good correlation between the change in mobility in terms of water rotational dynamics and the denaturation temperature of ribonuclease A. The changes in water dynamics due to osmolytes can be regarded as a pseudo-temperature-change, which agrees well with the change in protein denaturation temperature. These results indicate that the molecular dynamics of water around the protein is a key factor for protein denaturation.
MeSH term(s)	Molecular Dynamics Simulation ; Protein Denaturation ; Proteins/chemistry ; Temperature ; Thermodynamics ; Water/chemistry
Chemical Substances	Proteins ; Water (059QF0KO0R)
Language	English
Publishing date	2022-03-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1520-5207
ISSN (online)	1520-5207
DOI	10.1021/acs.jpcb.1c10634
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Article ; Online: Water Fraction Dependence of the Aggregation Behavior of Hydrophobic Fluorescent Solutes in Water-Tetrahydrofuran.

Tsuji, Hayato / Nakahata, Masaki / Hishida, Mafumi / Seto, Hideki / Motokawa, Ryuhei / Inoue, Takeru / Egawa, Yasunobu

The journal of physical chemistry letters

2023 Volume 14, Issue 49, Page(s) 11235–11241

Abstract: This work investigates the water fraction dependence of the aggregation behavior of hydrophobic solutes in water-tetrahydrofuran (THF) and the elucidation of the role of THF using fluorescence microscopy, dynamic light scattering, neutron and X-ray ... ...

Abstract	This work investigates the water fraction dependence of the aggregation behavior of hydrophobic solutes in water-tetrahydrofuran (THF) and the elucidation of the role of THF using fluorescence microscopy, dynamic light scattering, neutron and X-ray scattering, and photoluminescence measurements. On the basis of the obtained results, the following model is proposed: hydrophobic molecules are molecularly dispersed in the low-water-content region (10-20 vol %), while they form mesoscopic particles upon increasing the water fraction to ∼30 vol %. This abrupt change is due to the composition fluctuation of the water-THF binary system to form hydrophobic areas in THF, followed by THF-rich droplets where hydrophobic solutes are incorporated and form loose aggregates. Further increasing the water content prompts the desolvation of THF, which decreases the particle size and generates tight aggregates of solute molecules. This model is consistent with the luminescence behavior of the solutes and will be helpful to control the aggregation state of hydrophobic solutes in various applications.
Language	English
Publishing date	2023-12-07
Publishing country	United States
Document type	Journal Article
ISSN	1948-7185
ISSN (online)	1948-7185
DOI	10.1021/acs.jpclett.3c02882
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Article: Quasi-elastic neutron scattering reveals the relationship between the dynamical behavior of phospholipid headgroups and hydration water.

Rahman, Md Khalidur / Yamada, Takeshi / Yamada, Norifumi L / Hishida, Mafumi / Higuchi, Yuji / Seto, Hideki

Structural dynamics (Melville, N.Y.)

2023 Volume 10, Issue 4, Page(s) 44701

Abstract: The dynamics of hydration water (HW) in 1,2-dimyristoyl- ...

Abstract	The dynamics of hydration water (HW) in 1,2-dimyristoyl-
Language	English
Publishing date	2023-08-21
Publishing country	United States
Document type	Journal Article
ZDB-ID	2758684-4
ISSN	2329-7778
ISSN	2329-7778
DOI	10.1063/4.0000184
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Article ; Online: Rotational Dynamics of Water at the Phospholipid Bilayer Depending on the Head Groups Studied by Molecular Dynamics Simulations.

Higuchi, Yuji / Asano, Yuta / Kuwahara, Takuya / Hishida, Mafumi

Langmuir : the ACS journal of surfaces and colloids

2021 Volume 37, Issue 17, Page(s) 5329–5338

Abstract: Hydration states are a crucial factor that affect the self-assembly and properties of soft materials and biomolecules. Although previous experiments have revealed that the hydration state strongly depends on the chemical structure of lipid molecules, the ...

Abstract	Hydration states are a crucial factor that affect the self-assembly and properties of soft materials and biomolecules. Although previous experiments have revealed that the hydration state strongly depends on the chemical structure of lipid molecules, the mechanisms at the molecular level remain unknown. Classical and density-functional tight-binding (DFTB) molecular dynamics (MD) simulations are employed to determine the mechanisms underlying dissimilar water dynamics between lipid membranes with phosphatidylcholine (PC) and phosphatidylethanolamine (PE) head groups. The classical MD simulation shows that rotational relaxations of water are faster on the PE lipid than on the PC lipid, which is consistent with a previous experimental study using terahertz spectroscopy. Furthermore, DFTB-MD simulation of N(CH
Language	English
Publishing date	2021-04-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2005937-1
ISSN	1520-5827 ; 0743-7463
ISSN (online)	1520-5827
ISSN	0743-7463
DOI	10.1021/acs.langmuir.1c00417
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Article: Rotational Dynamics of Water at the Phospholipid Bilayer Depending on the Head Groups Studied by Molecular Dynamics Simulations

Higuchi, Yuji / Asano, Yuta / Kuwahara, Takuya / Hishida, Mafumi

Langmuir. 2021 Apr. 21, v. 37, no. 17

2021

Abstract	Hydration states are a crucial factor that affect the self-assembly and properties of soft materials and biomolecules. Although previous experiments have revealed that the hydration state strongly depends on the chemical structure of lipid molecules, the mechanisms at the molecular level remain unknown. Classical and density-functional tight-binding (DFTB) molecular dynamics (MD) simulations are employed to determine the mechanisms underlying dissimilar water dynamics between lipid membranes with phosphatidylcholine (PC) and phosphatidylethanolamine (PE) head groups. The classical MD simulation shows that rotational relaxations of water are faster on the PE lipid than on the PC lipid, which is consistent with a previous experimental study using terahertz spectroscopy. Furthermore, DFTB-MD simulation of N(CH₃)₄⁺ and NH₄⁺ ions, which correspond to the different head groups in PC and PE, respectively, shows qualitative agreement with the classical MD simulation. Remarkably, the PE lipids and the NH₄⁺ ions break hydrogen bonds between water molecules in the secondary hydration shell. In contrast, the PC lipids and the N(CH₃)₄⁺ ions bind water molecules weakly in both the primary and secondary hydration shells and increase hydrogen bonds between water. Our atomistic simulations show that these changes in the hydrogen-bond network of water molecules cause the different rotational relaxation of water molecules between the two lipids.
Keywords	chemical structure ; hydrogen ; hydrogen bonding ; molecular dynamics ; phosphatidylcholines ; phosphatidylethanolamines ; spectroscopy
Language	English
Dates of publication	2021-0421
Size	p. 5329-5338.
Publishing place	American Chemical Society
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	2005937-1
ISSN	1520-5827 ; 0743-7463
ISSN (online)	1520-5827
ISSN	0743-7463
DOI	10.1021/acs.langmuir.1c00417
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Article: Effect of Osmolytes on Water Mobility Correlates with Their Stabilizing Effect on Proteins

Hishida, Mafumi / Anjum, Rubaiya / Anada, Takahisa / Murakami, Daiki / Tanaka, Masaru

Journal of physical chemistry. 2022 Mar. 29, v. 126, no. 13

2022

Abstract	There is a long, ongoing debate on how small molecules (osmolytes) affect the stability of proteins. The present study found that change in collective rotational dynamics of water in osmolyte solutions likely has a dominant effect on protein denaturation. According to THz spectroscopy analysis, osmolytes that stabilize proteins are accompanied by bound hydration water with slow dynamics, while the collective rotational dynamics of water is accelerated in the case of denaturant osmolytes. Among 15 osmolytes studied here, there is a good correlation between the change in mobility in terms of water rotational dynamics and the denaturation temperature of ribonuclease A. The changes in water dynamics due to osmolytes can be regarded as a pseudo-temperature-change, which agrees well with the change in protein denaturation temperature. These results indicate that the molecular dynamics of water around the protein is a key factor for protein denaturation.
Keywords	denaturation ; molecular dynamics ; protein denaturation ; ribonucleases ; spectroscopy ; temperature
Language	English
Dates of publication	2022-0329
Size	p. 2466-2475.
Publishing place	American Chemical Society
Document type	Article
ISSN	1520-5207
DOI	10.1021/acs.jpcb.1c10634
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Article: Experimental Evidence of Slow Mode Water in the Vicinity of Poly(ethylene oxide) at Physiological Temperature

Tominaga, Taiki / Hishida, Mafumi / Murakami, Daiki / Fujii, Yoshihisa / Tanaka, Masaru / Seto, Hideki

Journal of physical chemistry. 2022 Feb. 23, v. 126, no. 8

2022

Abstract: In some synthetic polymers used for medical applications, hydration water in the vicinity of the polymer chains is known to play an important role in biocompatibility and is referred to as intermediate water. The crystallization of water below 0 °C ... ...

Abstract	In some synthetic polymers used for medical applications, hydration water in the vicinity of the polymer chains is known to play an important role in biocompatibility and is referred to as intermediate water. The crystallization of water below 0 °C observed during thermal analysis has been considered as evidence of the presence of intermediate water. However, the origin and physicochemical properties of intermediate water have not yet been elucidated. In this study, as a typical biocompatible polymer, poly(ethylene oxide) and its hydration water were investigated with the use of terahertz time-domain spectroscopy and quasi-elastic neutron scattering. The obtained results prove the existence of a significant amount of mobile water that interacts with the polymer chains even when the water content is low at physiological temperatures.
Keywords	biocompatibility ; crystallization ; neutrons ; spectroscopy ; temperature ; thermal analysis ; water content
Language	English
Dates of publication	2022-0223
Size	p. 1758-1767.
Publishing place	American Chemical Society
Document type	Article
ISSN	1520-5207
DOI	10.1021/acs.jpcb.1c09044
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Article ; Online: Experimental Evidence of Slow Mode Water in the Vicinity of Poly(ethylene oxide) at Physiological Temperature.

Tominaga, Taiki / Hishida, Mafumi / Murakami, Daiki / Fujii, Yoshihisa / Tanaka, Masaru / Seto, Hideki

The journal of physical chemistry. B

2022 Volume 126, Issue 8, Page(s) 1758–1767

Abstract	In some synthetic polymers used for medical applications, hydration water in the vicinity of the polymer chains is known to play an important role in biocompatibility and is referred to as intermediate water. The crystallization of water below 0 °C observed during thermal analysis has been considered as evidence of the presence of intermediate water. However, the origin and physicochemical properties of intermediate water have not yet been elucidated. In this study, as a typical biocompatible polymer, poly(ethylene oxide) and its hydration water were investigated with the use of terahertz time-domain spectroscopy and quasi-elastic neutron scattering. The obtained results prove the existence of a significant amount of mobile water that interacts with the polymer chains even when the water content is low at physiological temperatures.
MeSH term(s)	Ethylene Oxide ; Polyethylene Glycols/chemistry ; Polymers/chemistry ; Temperature ; Water/chemistry
Chemical Substances	Polymers ; Water (059QF0KO0R) ; Polyethylene Glycols (3WJQ0SDW1A) ; Ethylene Oxide (JJH7GNN18P)
Language	English
Publishing date	2022-02-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1520-5207
ISSN (online)	1520-5207
DOI	10.1021/acs.jpcb.1c09044
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