ブログ総もくじ 伏見啓明整形外科公式サイト Coロナ関連記事目次 今、電子カルテがあぶない 個人情報談義 目次
3. Results and Discussion
Various investigated natural products, their sources, and the type of antiviral activity reported against a variety of viruses are described in Table 1.
調査した様々な天然物、その供給源、および様々なウイルスに対して報告された抗ウイルス活性の種類を表1に示す。
The results acquired after
assessment of active site residues of SARS spike glycoprotein-Human ACE2 complex that may
be associated with the interaction with the ligand are shown in Figure 1.
リガンドとの相互作用に関連すると考えられるSARSスパイク糖タンパク質-ヒトACE2複合体の活性部位残基を評価した結果を図1に示す。
The binding interaction of the selected compounds with the SARS spike glycoprotein- Human ACE2 complex is characterized by their appropriate fitting in the binding pocket is shown in Figure 2.
選択された化合物のSARSスパイク糖タンパク質-ヒトACE2複合体との結合相互作用は、結合ポケットにおける適切なフィッティングによって特徴付けられ、図2に示されている。
The investigated natural products along with their 2D structures and the
docking results in terms of affinity (kcal/mol) and amino acid involved in the interaction of the
compound with the protein are shown in Figure 3.
調査した天然物について、その2次元構造、親和性（kcal/mol）および化合物とタンパク質との相互作用に関与するアミノ酸のドッキング結果を図3に示す。
And the binding potential of the compounds undergoing molecular docking is further evidenced by accompanying interaction (hydrogen bonds, pi-pi interaction, pi-alkyl interactions) with a variety of amino acid residues as represented in Table 2.
また、分子ドッキングを行った化合物の結合能は、表2に示すように、さまざまなアミノ酸残基との相互作用（水素結合、π-π相互作用、π-アルキル相互作用）を伴うことでさらに証明された。
Figure 1. Amino acid residues are existing in the active site of SARS spike glycoprotein-Human ACE2 complex along with chain “A” (green stick model), chain “B” (blue stick model), and chain “C” (orange stick model).
The binding sites of the SARS spike glycoprotein-Human ACE2 complex were determined in order to determine the amino acid residues, which may associate in the
interaction with ligand (Figure 1).
SARSスパイク糖タンパク質-ヒトACE2複合体の結合部位を決定した。（図1）。
The active amino acid residues were distributed in three chains A, B, and C, and active amino acid residues exist around the outer membrane of the crystal structure of protein rather than the inner core.
活性アミノ酸残基は3つの鎖A、B、Cに分布しており、活性アミノ酸残基はタンパク質の結晶構造の内核よりも外膜周辺に存在していた。
The docking study was performed to find the potential natural compounds accompanied by inhibitory properties towards the SARS spike glycoprotein-Human ACE2 complex with their individual binding affinity to the protein.
ドッキング研究は、SARSスパイク糖タンパク質-ヒトACE2複合体に対する阻害特性を伴う可能性のある天然化合物を、タンパク質に対する個々の結合親和性と共に見出すために行われた。
Since
the best binding interactions are accomplished when the affinity is least, indicating a highly
stabilized complex of the ligand and protein, this could be responsible for illicit the response.
Among the several natural candidates, the best affinity is associated in the case of indigo blue (-11.2 kcal/mol) followed by glycyrrhizin (-10.9 kcal/mol), β-sitosterol (-10.1 kcal/mol), indirubin (-9.8 kcal/mol), bicylogermacrene (-9.5 kcal/mol), curcumin (-9.3 kcal/mol), hesperetin (-9.2 kcal/mol), rhein (-9.1kcal/mol), berberine (-9.0 kcal/mol), chrysophanic acid (-8.8 kcal/mol), β-caryophyllene (-8.2 kcal/mol), and eugenol (-6.2 kcal/mol).
Figure 3. The residues of amino acids associated in the interaction of a) berberine, (b)indigo blue, (c) indirubin, (d) β-sitosterol, (e) glycyrrhizin, (f) hesperetin, (g) bicylogermacrene, (h) β-caryophyllene, (i) chrysophanic acid, (j) indirubin, (k) rhein, (l) curcumin and (m) eugenol with SARS spike glycoprotein-Human ACE2 complex.
Promising inhibitory activity of indigo blue towards the SARS spike glycoprotein- Human ACE2 complex was observed, which was associated with two hydrogen bonds with GLN 947 (Chain “A”) and GLN 744 (Chain “B”) respectively.
SARSスパイク糖タンパク質-ヒトACE2複合体に対するインジゴブルーの有望な阻害活性が観察され、これはそれぞれGLN 947（鎖 "A"）およびGLN 744（鎖 "B"）との2つの水素結合と関連していた。
A pi-pi stacked interaction with PHE 741 and a pi-sigma interaction with THR 943 (Chain “A”) was also observed.
PHE 741とのπ-πスタック相互作用、THR 943（鎖 "A"）とのπ-σ相互作用も観察された。
A prominent binding of glycyrrhizin was observed, which is associated with six hydrogen bonds, specifically with GLN 944, TYR 738, GLN 984, THR 980 (chain “A”), THR 980 (chain “B”), and ARG 977.
グリチルリチンの顕著な結合が観察され、これは6つの水素結合、具体的にはGLN 944、TYR 738、GLN 984、THR 980（鎖 "A"）、THR 980（鎖 "B"）およびARG 977と関連している。
It could be said that hydrogen bonds are the major interactions responsible for the prominent binding of glycyrrhizin with the SARS spike glycoprotein-Human ACE2 complex.
Table 2. Structure of natural products under investigation and their interactions with the amino acid residues and affinity in terms of kcal/mol.
4. Conclusions
0 件のコメント:
コメントを投稿