親水性アミノ酸

WordNet

street name for lysergic acid diethylamide (同)back breaker, battery-acid, dose, dot, Elvis, loony toons, Lucy in the sky with diamonds, pane, superman, window pane, Zen
any of various water-soluble compounds having a sour taste and capable of turning litmus red and reacting with a base to form a salt
having the characteristics of an acid; "an acid reaction"
pertaining to or containing any of a group of organic compounds of nitrogen derived from ammonia (同)aminic
the radical -NH2 (同)amino_group
having a strong affinity for water; tending to dissolve in, mix with, or be wetted by water

PrepTutorEJDIC

酸性の / 酸味のある,すっぱい(sour) / (言葉・態度などが)厳しい,しんらつな / 酸 / すっぱいもの / 《俗》=LSD

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1. フェニルケトン尿症の概要 overview of phenylketonuria
2. 乳児および小児における低血糖に対するアプローチ approach to hypoglycemia in infants and children
3. 先天性代謝異常：分類 inborn errors of metabolism classification
4. 尿素サイクル障害：臨床的特徴および診断 urea cycle disorders clinical features and diagnosis
5. 先天性代謝異常：代謝性救急疾患 inborn errors of metabolism metabolic emergencies

English Journal

Comparative analysis of binary and ternary cyclodextrin complexes with econazole nitrate in solution and in solid state.

Jug M1, Mennini N2, Kövér KE3, Mura P2.Author information 1Department of Pharmaceutical Technology, Faculty of Pharmacy and Biochemistry, University of Zagreb, A. Kovačića 1, Zagreb 10000 HR, Croatia. Electronic address: mjug@pharma.hr.2Department of Pharmaceutical Sciences, Faculty of Pharmacy, University of Florence, via Schiff 6, Sesto Fiorentino 50019, Florence, Italy.3Department of Inorganic and Analytical Chemistry, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1., Debrecen 4010, Hungary.AbstractThe aim of this work was to investigate in-depth interactions of econazole nitrate (ECN), a very poorly water-soluble antifungal agent, with different β-cyclodextrin (βCD) derivatives, and to evaluate the potential synergistic effect of suitable third compounds (l-amino acids, citric acid, hydrophilic polymers). Phase-solubility studies showed the formation of equimolar complexes with all tested CDs, and indicated sulfobutyl-βCD (SBEβCD) as the best complexing and solubilizing agent for ECN, followed by hydroxypropyl-βCD (HPβCD). 1D and 2D (1)H NMR studies demonstrated the actual formation of inclusion complexes of 1:1mol:mol stoichiometry, and gave insight about different inclusion modes of ECN molecule into the CD cavity, simultaneously existing in solution. Among the different tested ternary systems, only those with citric acid (CA) enabled a significant increase in complexing and solubilizing ability towards the drug with respect to the binary ones, indicating a synergistic effect between SBEβCD and CA and the formation of highly soluble ternary complexes, which was further supported by NMR studies. Solid equimolar binary and ternary systems of ECN, CDs and CA were prepared by co-grinding in high energy vibrational micro-mills and characterized by differential scanning calorimetry, X-ray powder diffractometry and in vitro dissolution studies. In the case of binary systems, total sample amorphization, indicative of strong solid state interactions and possible inclusion complex formation, was obtained only for co-ground products with HPβCD and SBEβCD, but they both presented a dissolution profile typical of a supersaturated system, with a limited improvement of drug dissolution efficiency (8.3 and 22.13 times, respectively). On the contrary, the ternary ECN/SBEβCD/CA co-ground product presented superior dissolution properties, increasing the ECN dissolution efficiency of 66.62 times, clearly having the best potential for further development of a novel ECN delivery system for efficient delivery of the drug to the oral cavity, thus improving the therapy of oral candidosis.
Journal of pharmaceutical and biomedical analysis.J Pharm Biomed Anal.2014 Mar 25;91:81-91. doi: 10.1016/j.jpba.2013.12.029. Epub 2014 Jan 2.
The aim of this work was to investigate in-depth interactions of econazole nitrate (ECN), a very poorly water-soluble antifungal agent, with different β-cyclodextrin (βCD) derivatives, and to evaluate the potential synergistic effect of suitable third compounds (l-amino acids, citric acid, hydroph
PMID 24444785

Unique Crystal Structure of a Novel Surfactant Protein from the Foam Nest of the Frog Leptodactylus vastus.

Cavalcante Hissa D, Arruda Bezerra G, Birner-Gruenberger R, Paulino Silva L, Usón I, Gruber K, Maciel Melo VM.Author information Lab. de Ecologia Microbiana e Biotecnologia-LEMBiotech, Departamento de Biologia, Universidade Federal do Ceará, Av. Humberto Monte 2977, Campus do Pici, Bloco 909, Fortaleza, CE, 60455-000 (Brazil).AbstractBreeding by releasing eggs into stable biofoams ("foam nests") is a peculiar reproduction mode within anurans, fish, and tunicates; not much is known regarding the biochemistry or molecular mechanisms involved. Lv-ranaspumin (Lv-RSN-1) is the predominant protein from the foam nest of the frog Leptodactylus vastus. This protein shows natural surfactant activity, which is assumed to be crucial for stabilizing foam nests. We elucidated the amino acid sequence of Lv-RSN-1 by de novo sequencing with mass-spectrometry and determined the high-resolution X-ray structure of the protein. It has a unique fold mainly composed of a bundle of 11 α-helices and two small antiparallel β-strands. Lv-RSN-1 has a surface rich in hydrophilic residues and a lipophilic cavity in the region of the antiparallel β-sheet. It possesses intrinsic surface-active properties, reducing the surface tension of water from 73 to 61 mN m(-1) (15 μg mL(-1) ). Lv-RSN-1 belongs to a new class of surfactants proteins for which little has been reported regarding structure or function.
Chembiochem : a European journal of chemical biology.Chembiochem.2014 Feb 10;15(3):393-8. doi: 10.1002/cbic.201300726. Epub 2014 Jan 17.
Breeding by releasing eggs into stable biofoams ("foam nests") is a peculiar reproduction mode within anurans, fish, and tunicates; not much is known regarding the biochemistry or molecular mechanisms involved. Lv-ranaspumin (Lv-RSN-1) is the predominant protein from the foam nest of the frog Leptod
PMID 24442854

Amino acid similarities and divergences in the small surface proteins of genotype C hepatitis B viruses between nucleos(t)ide analogue-naïve and lamivudine-treated patients with chronic hepatitis B.

Ding H1, Liu B2, Zhao C1, Yang J1, Yan C1, Yan L1, Zhuang H1, Li T3.Author information 1Department of Microbiology and Infectious Disease Center, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Haidian District, Beijing 100191, PR China.2Department of Microbiology and Infectious Disease Center, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Haidian District, Beijing 100191, PR China; Department of Microbiology, Immunology and Biochemistry, University of Tennessee Health Science Center, Memphis, TN 38163, USA.3Department of Microbiology and Infectious Disease Center, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Haidian District, Beijing 100191, PR China. Electronic address: tongli08@vip.sina.com.AbstractEntire C-genotype small hepatitis B surface (SHBs) sequences were isolated from 139 nucleos(t)ide analogues (NA)-naïve and 74 lamivudine (LMV)-treated chronic hepatitis B (CHB) patients. The conservation and variability of total 226 amino acids (AAs) within the sequences were determined individually, revealing significant higher mutant isolate rate and mutation frequency in LMV-treated cohort than those in the NA-naïve one (P=0.009 and 0.0001, respectively). Three absolutely conserved fragments (s16-s19, s176-s181 and s185-s188) and seven moderately conserved regions (a few AA sites acquiring increased variability after LMV-treatment) were identified. The significant mutation rate increase after LMV-treatment occurred primarily in major hydrophilic region (except 'a' determinant) and transmembrane domain 3/4, but not in other upstream functional regions of SHBs. With little influence on immune escape-associated mutation frequencies within 'a' determinant, LMV-monotherapy significantly induced classical LMVr-associated mirror changes sE164D/rtV173L, sI195M/rtM204V and sW196L/S/rtM204I, as well as non-classical ones sG44E/rtS53N, sT47K/A/rtH55R/Q and sW182stop/rtV191I outside 'a' determinant. Interestingly, another newly-identified truncation mutation sC69stop/rtS78T decreased from 7.91% (11/139) in NA-naïve cohort to 2.70% (2/74) in LMV-treated one. Altogether, the altered AA conservation and diversity in SHBs sequences after LMV-treatment in genotype-C HBV infection might shed new insights into how LMV-therapy affects the SHBs variant evolution and its antigenicity.
Antiviral research.Antiviral Res.2014 Feb;102:29-34. doi: 10.1016/j.antiviral.2013.11.015. Epub 2013 Dec 4.
Entire C-genotype small hepatitis B surface (SHBs) sequences were isolated from 139 nucleos(t)ide analogues (NA)-naïve and 74 lamivudine (LMV)-treated chronic hepatitis B (CHB) patients. The conservation and variability of total 226 amino acids (AAs) within the sequences were determined individuall
PMID 24316031

Japanese Journal

Metabolomics-based component profiling of hard and semi-hard natural cheeses with gas chromatography/time-of-flight-mass spectrometry, and its application to sensory predictive modeling(BREWING AND FOOD TECHNOLOGY)

Ochi Hiroshi,Naito Hiroshige,Iwatsuki Keiji,Bamba Takeshi,Fukusaki Eiichiro
Journal of bioscience and bioengineering 113(6), 751-758, 2012-06
… Gas chromatography/time-of-flight mass spectrometry (GC/TOF-MS) was used to analyze hydrophilic low molecular weight components, including amino acids, fatty acids, amines, organic acids, and saccharides, in cheese, and the sensometric application for practical metabolomic studies in the food industry is described. …
NAID 110009470598

Identification of a New IgE-Binding Epitope of Peanut Oleosin That Cross-Reacts with Buckwheat

KOBAYASHI Shoko,KATSUYAMA Shinta,WAGATSUMA Tamae,OKADA Shinji,TANABE Soichi
Bioscience, Biotechnology, and Biochemistry 76(6), 1182-1188, 2012
… Based on the amino acid sequence and mass spectrometric analysis data, the peptide was identified as Ser-Asp-Gln-Thr-Arg-Thr-Gly-Tyr (SDQTRTGY); … this sequence is identical to amino acids 2–9 in the N-terminal hydrophilic domain of oleosin 3 which is located on the surface of the lipid storage body. …
NAID 130001862811

Isoleucine 259 and isoleucine 260 residues in Streptococcus gordonii soluble inorganic pyrophosphatase play an important role in enzyme activity(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

Ilias Mohammad,White Scott A.,Young Tom W.
Journal of bioscience and bioengineering 112(1), 8-13, 2011-07
… Amino acid residues isoleudne 259 (I259) and isoleucine 260 (I260) are highly conserved among catalytically active family II PPases and are located very close to the hinge region. … Substitution of either I259 or I260 with a hydrophilic acidic amino acid (glutamate or aspartate) resulted in adverse effects on the kinetic properties of the enzyme. …
NAID 110008686236