Coordination chemistry of Ca sites at the surface of nanosized hydroxyapatite: interaction with H₂O and CO.
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Coordination chemistry of Ca sites at the surface of nanosized hydroxyapatite: interaction with H₂O and CO.
Affinity to water well-defined selection, nanostructured hydroxyapatite (HA) samples were investigated by H (2) O vapor adsorption microcalorimetry and infrared (IR) spectroscopy. A great all the materials investigated hydrophilicity confirmed. Surface features of the hydrated HA investigated in the as-synthesized samples pre-treated under mild conditions at T = 303 K, while the HA features dehydration marked on the sample activated at T = 573 K.
The relative hydrophilicity of the surface hydrated (-Δ (ad) H ~ 100-50 kJ mol (-1)) is due to the interaction of water with a very polarized H (2) O molecule highly coordinated to the surface of Ca (2+) cations. On the surface dehydration, showing coordinative unsaturated (cus) Ca (2+) cation, H (2) O is the molecular adsorbed but more powerful (-Δ (ad) H ~ 120-90 kJ mol (-1)). The use of CO adsorption for measuring Lewis acid strength of the HA surface sites revealed only moderate force cus Ca (2+) cations, as confirmed by a second measurement microcalorimetric and IR spectroscopy and ab initio calculations.
These results indicate that HA / H (2) O great interaction energy is caused by the interaction between cus Ca (2+) site and the nearest PO hydrophilic (4) group, were not disclosed by the probe CO. Low density cus Ca (2+) cations at 573 K is activated HA surface with respect to one of pure does not affect the entire hydrophilicity of the surface, as the polarizing effect of Ca sites so strong as to extend up to four layers of hydrated, as confirmed by both microcalorimetric-high coverage and the data of IR spectroscopy. There are no special effects for specimens investigated methods of preparation and / or a different morphology were observed.
Coordination chemistry of Ca sites at the surface of nanosized hydroxyapatite: interaction with H₂O and CO.
Revisiting the alkaline earth metal isoreticular MOFs: a comprehensive study of phase stability, electronic structure, chemical bonding, and optical properties of A-IRMOF-1 (A = Be, Mg, Ca, Sr, Ba).
energy of formation, chemical bonds, the electronic structure and optical properties of the metal framework-organic alkaline earth metal, A-IRMOF-1 (where A = Be, Mg, Ca, Sr, or Ba), has been systematically investigated by the method of DFT , The volume of the unit cell and atomic positions are fully optimized with PERDEW-Burke-Ernzerhof functional. By fitting the data E-V into the equation Murnaghan, Birch and Universal countries (UEOS), the bulk modulus and its pressure derivative is expected and give almost the same results.
Data show that the series A-IRMOF-1 is a soft material. the estimated value of all the band gap of ca. 3.5 eV, a non-metallic exhibiting behavior that is essentially independent of this metal in the series A-IRMOF-1. formation energy calculated for the A-IRMOF-1 series -61.69 (Be), -62.53 (Mg), -66.56 (Ca), -65.34 (Sr), and -64.12 (Ba) kJ mol (-1) and substantially more negative than Zn based IRMOF-1 (MOF-5) at -46.02 kJ mol (-1). From the viewpoint of thermodynamics, the compound A-IRMOF-1 therefore even more stable than the famous MOF-5. Linear optical properties of the series A-IRMOF-1 systematically investigated.
The detailed analysis of the chemical bonds in the series A-IRMOF-1 reveals the nature of A-O, O-C, H-C and C-C bond, ie, A-O is primarily ionic interaction with metal dependence Covalency level. O-C, H-C and C-C bond interaction is as anticipated mainly covalent in character. Furthermore, it was found that the geometry and electronic structure of MOFs is now considered to be very sensitive to the k-point mesh involved in the calculation.
Description: Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, a vasodilator. Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin. Also cleaves other biological peptides, such as apelins, casomorphins and dynorphin A with high efficiency. In addition, ACE2 C-terminus is homologous to collectrin and is responsible for the trafficking of the neutral amino acid transporter SL6A19 to the plasma membrane of gut epithelial cells via direct interaction, regulating its expression on the cell surface and its catalytic activity.
Description: ACE2 Antibody: Angiotensin-converting enzyme 2 (ACE2) plays a central role in vascular, renal, and myocardial physiology. In contrast to its homolog ACE, ACE2 expression is restricted to heart, kidney, and testis. Recently. ACE2 has also been shown to be a functional receptor of the SARS coronavirus. Homology modeling shows 2019-nCoV has a similar receptor-binding domain structure as SARS-CoV, which suggests COVID-19 (2019-nCoV) may use ACE2 as a receptor in humans for infection. The normal function of ACE2 is to convert the inactive vasoconstrictor angiotensin I (AngI) to Ang1-9 and the active form AngII to Ang1-7, unlike ACE, which converts AngI to AngII. While the role of these vasoactive peptides is not well understood, lack of ACE2 expression in ace2-/ace2- mice leads to severely reduced cardiac contractility, indicating its importance in regulating heart function.
Description: ACE2 Antibody: Angiotensin-converting enzyme 2 (ACE2) plays a central role in vascular, renal, and myocardial physiology. In contrast to its homolog ACE, ACE2 expression is restricted to heart, kidney, and testis. Recently. ACE2 has also been shown to be a functional receptor of the SARS coronavirus. Homology modeling shows 2019-nCoV has a similar receptor-binding domain structure as SARS-CoV, which suggests COVID-19 (2019-nCoV) may use ACE2 as a receptor in humans for infection. The normal function of ACE2 is to convert the inactive vasoconstrictor angiotensin I (AngI) to Ang1-9 and the active form AngII to Ang1-7, unlike ACE, which converts AngI to AngII. While the role of these vasoactive peptides is not well understood, lack of ACE2 expression in ace2-/ace2- mice leads to severely reduced cardiac contractility, indicating its importance in regulating heart function.
Description: ACE2 Antibody: Angiotensin-converting enzyme 2 (ACE2) plays a central role in vascular, renal, and myocardial physiology. In contrast to its homolog ACE, ACE2 expression is restricted to heart, kidney, and testis. Recently. ACE2 has also been shown to be a functional receptor of the SARS coronavirus. Homology modeling shows 2019-nCoV has a similar receptor-binding domain structure as SARS-CoV, which suggests COVID-19 (2019-nCoV) may use ACE2 as a receptor in humans for infection. The normal function of ACE2 is to convert the inactive vasoconstrictor angiotensin I (AngI) to Ang1-9 and the active form AngII to Ang1-7, unlike ACE, which converts AngI to AngII. While the role of these vasoactive peptides is not well understood, lack of ACE2 expression in ace2-/ace2- mice leads to severely reduced cardiac contractility, indicating its importance in regulating heart function.
Description: ACE2 Antibody: Angiotensin-converting enzyme 2 (ACE2) plays a central role in vascular, renal, and myocardial physiology. In contrast to its homolog ACE, ACE2 expression is restricted to heart, kidney, and testis. Recently. ACE2 has also been shown to be a functional receptor of the SARS coronavirus. Homology modeling shows 2019-nCoV has a similar receptor-binding domain structure as SARS-CoV, which suggests COVID-19 (2019-nCoV) may use ACE2 as a receptor in humans for infection. The normal function of ACE2 is to convert the inactive vasoconstrictor angiotensin I (AngI) to Ang1-9 and the active form AngII to Ang1-7, unlike ACE, which converts AngI to AngII. While the role of these vasoactive peptides is not well understood, lack of ACE2 expression in ace2-/ace2- mice leads to severely reduced cardiac contractility, indicating its importance in regulating heart function.
Description: ACE2 Antibody: Angiotensin-converting enzyme 2 (ACE2) plays a central role in vascular, renal, and myocardial physiology. In contrast to its homolog ACE, ACE2 expression is restricted to heart, kidney, and testis. Recently. ACE2 has also been shown to be a functional receptor of the SARS coronavirus. Homology modeling shows 2019-nCoV has a similar receptor-binding domain structure as SARS-CoV, which suggests COVID-19 (2019-nCoV) may use ACE2 as a receptor in humans for infection. The normal function of ACE2 is to convert the inactive vasoconstrictor angiotensin I (AngI) to Ang1-9 and the active form AngII to Ang1-7, unlike ACE, which converts AngI to AngII. While the role of these vasoactive peptides is not well understood, lack of ACE2 expression in ace2-/ace2- mice leads to severely reduced cardiac contractility, indicating its importance in regulating heart function.
Description: ACE2 Antibody: Angiotensin-converting enzyme 2 (ACE2) plays a central role in vascular, renal, and myocardial physiology. In contrast to its homolog ACE, ACE2 expression is restricted to heart, kidney, and testis. Recently. ACE2 has also been shown to be a functional receptor of the SARS coronavirus. Homology modeling shows 2019-nCoV has a similar receptor-binding domain structure as SARS-CoV, which suggests COVID-19 (2019-nCoV) may use ACE2 as a receptor in humans for infection. The normal function of ACE2 is to convert the inactive vasoconstrictor angiotensin I (AngI) to Ang1-9 and the active form AngII to Ang1-7, unlike ACE, which converts AngI to AngII. While the role of these vasoactive peptides is not well understood, lack of ACE2 expression in ace2-/ace2- mice leads to severely reduced cardiac contractility, indicating its importance in regulating heart function.
Description: ACE2 Antibody: Angiotensin-converting enzyme 2 (ACE2) plays a central role in vascular, renal, and myocardial physiology. In contrast to its homolog ACE, ACE2 expression is restricted to heart, kidney, and testis. Recently. ACE2 has also been shown to be a functional receptor of the SARS coronavirus. Homology modeling shows 2019-nCoV has a similar receptor-binding domain structure as SARS-CoV, which suggests COVID-19 (2019-nCoV) may use ACE2 as a receptor in humans for infection. The normal function of ACE2 is to convert the inactive vasoconstrictor angiotensin I (AngI) to Ang1-9 and the active form AngII to Ang1-7, unlike ACE, which converts AngI to AngII. While the role of these vasoactive peptides is not well understood, lack of ACE2 expression in ace2-/ace2- mice leads to severely reduced cardiac contractility, indicating its importance in regulating heart function.
Description: ACE2 Antibody: Angiotensin-converting enzyme 2 (ACE2) plays a central role in vascular, renal, and myocardial physiology. In contrast to its homolog ACE, ACE2 expression is restricted to heart, kidney, and testis. Recently. ACE2 has also been shown to be a functional receptor of the SARS coronavirus. Homology modeling shows 2019-nCoV has a similar receptor-binding domain structure as SARS-CoV, which suggests COVID-19 (2019-nCoV) may use ACE2 as a receptor in humans for infection. The normal function of ACE2 is to convert the inactive vasoconstrictor angiotensin I (AngI) to Ang1-9 and the active form AngII to Ang1-7, unlike ACE, which converts AngI to AngII. While the role of these vasoactive peptides is not well understood, lack of ACE2 expression in ace2-/ace2- mice leads to severely reduced cardiac contractility, indicating its importance in regulating heart function.
Description: A polyclonal antibody against ACE2. Recognizes ACE2 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, IHC;ELISA:1:2000-1:5000, IHC:1:25-1:100
Description: A polyclonal antibody against ACE2. Recognizes ACE2 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, IHC;ELISA:1:2000-1:10000, IHC:1:100-1:300
Description: A polyclonal antibody against ACE2. Recognizes ACE2 from Human, Mouse. This antibody is Unconjugated. Tested in the following application: WB, ELISA;WB:1/500-1/2000.ELISA:1/40000
Description: A polyclonal antibody against ACE2. Recognizes ACE2 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, IHC;ELISA:1:1000-1:5000, IHC:1:25-1:100
Description: Human Angiotensin converting enzyme 2 (ACE2), also known as ACEH, is an integral membrane protein found on the surface of cells in the lungs, arteries, heart, kidney, and intestines. ACE2 serves as the entry point into cells for some coronaviruses, including the two strains that caused outbreaks of Severe acute respiratory syndrome (SARS-CoV) and coronavirus disease 2019 (COVID-19) (SARS-CoV-2)._x000D_ The ACE2 Lentivirus are replication incompetent, HIV-based, VSV-G pseudotyped lentiviral particles that are ready to be transduced into almost all types of mammalian cells, including primary and non-dividing cells. The particles contain an ACE2 gene (NM_021804.3) driven by an EF1a promoter._x000D_ _x000D_
Description: Human Angiotensin converting enzyme 2 (ACE2) also known ACEH, GenBank Accession No. NP_068576.1, a.a. 18-740, with a C-terminal His-tag, expressed in a HEK293 expression system. MW=85 kDa.
Description: Human Angiotensin converting enzyme 2 (ACE2) also known ACEH, GenBank Accession No. NP_068576.1, a.a. 18-740, with a C-terminal His-tag, expressed in a HEK293 expression system. MW=85 kDa.
Importantly, this indicates that the sample with the Γ-point will only provide reliable structural properties of MOFs. Thus, the computational simulation should be readily extended to the MOF system even more complicated.
