Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Drug
Enzyme
Compound
Query: UMLS:C0012739 (
disseminated intravascular coagulation
)
8,673
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Our mutational studies on Hb S showed that the Hb S beta73His variant (beta6Val and beta73His) promoted polymerization, while Hb S beta73Leu (beta6Val and beta73Leu) inhibited polymerization. On the basis of these results, we speculated that EF-helix peptides containing beta73His interact with beta4Thr in Hb S and compete with Hb S, resulting in inhibition of Hb S polymerization. We, therefore, studied inhibitory effects of 15-, 11-, 7-, and 3-
mer
EF-helix peptides containing beta73His on Hb S polymerization. The delay time prior to Hb S polymerization increased only in the presence of the 15-
mer
His peptide; the higher the amount, the longer the delay time.
DIC
image analysis also showed that the fiber elongation rate for Hb S polymers decreased with increasing concentration of the 15-
mer
His peptide. In contrast, the same 15-
mer
peptide containing beta73Leu instead of His and peptides shorter than 11 amino acids containing beta73His including His alone showed little effect on the kinetics of polymerization and elongation of polymers. Analysis by protein-chip arrays showed that only the 15-
mer
beta73His peptide interacted with Hb S. CD spectra of the 15-
mer
beta73His peptide did not show a specific helical structure; however, computer docking analysis suggested a lower energy for interaction of Hb S with the 15-
mer
beta73His peptide compared to peptides containing other amino acids at this position. These results suggest that the 15-
mer
beta73His peptide interacts with Hb S via the beta4Thr in the betaS-globin chain in Hb S. This interaction may influence hydrogen bond interaction between beta73Asp and beta4Thr in Hb S polymers and interfere in hydrophobic interactions of beta6Val, leading to inhibition of Hb S polymerization.
...
PMID:Inhibition of hemoglobin S polymerization in vitro by a novel 15-mer EF-helix beta73 histidine-containing peptide. 1681 35
Standard linear Fmoc/t-Bu solid-phase synthesis of the 42-
mer
beta-amyloid (1-42) peptide was achieved under controlled microwave conditions at 86 degrees C using inexpensive
DIC
/HOBt as coupling reagent on ChemMatrix resin. In order to avoid racemization of the sensitive amino acids, the coupling of the three His residues in the difficult peptide sequence was performed at room temperature. The desired peptide was obtained within 15 h overall processing time in high yield and purity (78% crude yield).
...
PMID:Direct solid-phase synthesis of the beta-amyloid (1-42) peptide using controlled microwave heating. 2018 May 52